Psychrophiles thriving permanently at near-zero temperatures synthesize cold-active enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, therefore reducing the free energy barrier of the transition state. Furthermore, a weak temperature dependence of activity ensures moderate reduction of the catalytic activity in the cold. In these naturally evolved enzymes, the optimization to low temperature activity is reached via destabilization of the structures bearing the active site or by destabilization of the whole molecule. This involves a reduction in the number and strength of all types of weak interactions or the disappearance of stability factors, resulting in improved dynamics of active site residues in the cold. These enzymes are already used in many biotechnological applications requiring high activity at mild temperatures or fast heat-inactivation rate. Several open questions in the field are also highlighted. 1. Introduction “Coping with our cold planet” [1], the title of this recent review unambiguously stresses a frequently overlooked aspect: the Earth’s biosphere is predominantly cold and permanently exposed to temperatures below 5°C. Such low mean temperature mainly arises from the fact that 71% of the Earth’s surface is covered by oceans that have a constant temperature of 2–4°C below 1000？m depth, irrespective of the latitude. The polar regions account for another 15%, to which the glacier and alpine regions must be added as well as the permafrost representing more than 20% of terrestrial soils. Although inhospitable, all these low temperature biotopes have been successfully colonized by cold-adapted organisms (Figure 1). Psychrophiles thrive in permanently cold environments (in thermal equilibrium with the medium) and even at subzero temperatures in supercooled liquid water. Such extremely cold conditions are encountered, for instance, in salty cryopegs at ？10°C in the Arctic permafrost [2, 3], in the brine veins between polar sea ice crystals at ？20°C [4–6], or in supercooled cloud droplets [7, 8]. Unusual microbiotopes have also been described, such as porous rocks in Antarctic dry valleys hosting microbial communities surviving at ？60°C [9, 10]. Cryoconite holes on glacier surfaces represent another permanently cold biotope hosting complex microbial communities [11, 12]. These
References
[1]
D. F. Rodrigues and J. M. Tiedje, “Coping with our cold planet,” Applied and Environmental Microbiology, vol. 74, no. 6, pp. 1677–1686, 2008.
[2]
D. Gilichinsky, E. Rivkina, C. Bakermans et al., “Biodiversity of cryopegs in permafrost,” FEMS Microbiology Ecology, vol. 53, no. 1, pp. 117–128, 2005.
[3]
B. Steven, R. Léveillé, W. H. Pollard, and L. G. Whyte, “Microbial ecology and biodiversity in permafrost,” Extremophiles, vol. 10, no. 4, pp. 259–267, 2006.
[4]
J. W. Deming, “Psychrophiles and polar regions,” Current Opinion in Microbiology, vol. 5, no. 3, pp. 301–309, 2002.
[5]
K. Junge, H. Eicken, and J. W. Deming, “Bacterial activity at -2 to -20°C in arctic wintertime sea ice,” Applied and Environmental Microbiology, vol. 70, no. 1, pp. 550–557, 2004.
[6]
C. Bakermans and M. L. Skidmore, “Microbial metabolism in ice and brine at -5°C,” Environmental Microbiology, vol. 13, pp. 2269–2278, 2011.
[7]
B. Sattler, H. Puxbaum, and R. Psenner, “Bacterial growth in supercooled cloud droplets,” Geophysical Research Letters, vol. 28, no. 2, pp. 239–242, 2001.
[8]
M. Va？tilingom, P. Amato, M. Sancelme, P. Laj, M. Leriche, and A. M. Delort, “Contribution of microbial activity to carbon chemistry in clouds,” Applied and Environmental Microbiology, vol. 76, no. 1, pp. 23–29, 2010.
[9]
E. I. Friedmann, “Endolithic microorganisms in the Antarctic cold desert,” Science, vol. 215, no. 4536, pp. 1045–1053, 1982.
[10]
S. C. Cary, I. R. McDonald, J. E. Barrett, and D. A. Cowan, “On the rocks: the microbiology of Antarctic Dry Valley soils,” Nature Reviews Microbiology, vol. 8, no. 2, pp. 129–138, 2010.
[11]
M. Stibal, M. ？abacká, and K. Ka？tovská, “Microbial communities on glacier surfaces in Svalbard: impact of physical and chemical properties on abundance and structure of cyanobacteria and algae,” Microbial Ecology, vol. 52, no. 4, pp. 644–654, 2006.
[12]
K. A. Cameron, A. J. Hodson, and A. M. Osborn, “Structure and diversity of bacterial, eukaryotic and archaeal communities in glacial cryoconite holes from the Arctic and the Antarctic,” FEMS Microbiology Ecology, vol. 82, no. 2, pp. 254–267, 2012.
[13]
R. Y. Morita, “Psychrophilic bacteria,” Bacteriological reviews, vol. 39, no. 2, pp. 144–167, 1975.
[14]
N. J. Russell, “Cold adaptation of microorganisms,” Philosophical Transactions of the Royal Society, vol. 326, pp. 595–611, 1990.
[15]
A. M. Gounot, “Bacterial life at low temperature: physiological aspects and biotechnological implications,” Journal of Applied Bacteriology, vol. 71, no. 5, pp. 386–397, 1991.
[16]
N. J. Russell, “Molecular adaptations in psychrophilic bacteria: potential for biotechnological applications,” Advances in Biochemical Engineering/Biotechnology, vol. 61, pp. 1–21, 1998.
[17]
R. Cavicchioli, “Cold-adapted archaea,” Nature Reviews Microbiology, vol. 4, no. 5, pp. 331–343, 2006.
[18]
R. M. Morgan-Kiss, J. C. Priscu, T. Pocock, L. Gudynaite-Savitch, and N. P. A. Huner, “Adaptation and acclimation of photosynthetic microorganisms to permanently cold environments,” Microbiology and Molecular Biology Reviews, vol. 70, no. 1, pp. 222–252, 2006.
[19]
P. Buzzini, E. Branda, M. Goretti, and B. Turchetti, “Psychrophilic yeasts from worldwide glacial habitats: diversity, adaptation strategies and biotechnological potential,” FEMS Microbiology Ecology, vol. 82, no. 2, pp. 217–241, 2012.
[20]
R. Margesin, G. Neuner, and K. B. Storey, “Cold-loving microbes, plants, and animals—fundamental and applied aspects,” Naturwissenschaften, vol. 94, no. 2, pp. 77–99, 2007.
[21]
D. Doucet, V. K. Walker, and W. Qin, “The bugs that came in from the cold: molecular adaptations to low temperatures in insects,” Cellular and Molecular Life Sciences, vol. 66, no. 8, pp. 1404–1418, 2009.
[22]
J. T. Eastman, Antarctic Fish Biology: Evolution in a Unique Environment, Academic Press, San Diego, Calif, USA, 1993.
[23]
G. di Prisco, E. Pisano, and A. Clarke, Fishes of AntarcticA: A Biological Overview, Springer, Milano, Italy, 1998.
[24]
D. Giordano, R. Russo, G. di Prisco, and C. Verde, “Molecular adaptations in Antarctic fish and marine microorganisms,” Marine Genomics, vol. 6, pp. 1–6, 2012.
[25]
C. R. Dial, R. J. Dial, R. Saunders et al., “Historical biogeography of the North American glacier ice worm, Mesenchytraeus solifugus (Annelida: Oligochaeta: Enchytraeidae),” Molecular Phylogenetics and Evolution, vol. 63, pp. 577–584, 2012.
[26]
R. Margesin and F. Schinner, Cold-Adapted Organisms: Ecology, Physiology, Enzymology and Molecular Biology, Springer, Heidelberg, Germany, 1999.
[27]
C. Gerday and N. Glansdorff, Physiology and Biochemistry of Extremophiles, ASM Press, Washington, DC, USA, 2007.
[28]
R. Margesin, F. Schinner, J. C. Marx, and C. Gerday, Psychrophiles, from Biodiversity to Biotechnology, Springer, Berlin, Germany, 2008.
[29]
K. Horikoshi, G. Antranikian, A. T. Bull, F. T. Robb, and K. O. Stetter, Eds., Extremophiles Handbook, Springer, Berlin, Germany, 2011.
[30]
R. V. Miller and L. G. Whyte, Polar Microbiology. Life in a Deep Freeze, ASM Press, Washington, DC, USA, 2012.
[31]
R. Margesin, G. Feller, C. Gerday, and N. J. Russell, “Cold-adapted microorganisms: adaptation strategies and biotechnological potential,” in EncyclopEdia of Environmental Microbiology, G. Bitton, Ed., pp. 871–885, John Wiley & Sons, New York, NY, USA, 2002.
[32]
S. D'Amico, T. Collins, J. C. Marx, G. Feller, and C. Gerday, “Psychrophilic microorganisms: challenges for life,” EMBO Reports, vol. 7, no. 4, pp. 385–389, 2006.
[33]
B. Methé, K. E. Nelson, and C. M. Fraser, “It's a cold world out there (but the prospects are hot),” Trends in Microbiology, vol. 12, no. 12, pp. 532–534, 2004.
[34]
A. Danchin, “An interplay between metabolic and physicochemical constrains: lessons from the psychrophilic prokaryote genomes,” in Physiology and Biochemistry of Extremophiles, C. Gerday and N. Glansdorff, Eds., pp. 208–220, ASM Press, Washington, DC, USA, 2007.
[35]
J. B. Bowman, “Genomic analysis of psychrophilic prokaryotes,” in Psychrophiles, from Biodiversity to Biotechnology, R. Margesin, F. Schinner, J. C. Marx, and C. Gerday, Eds., pp. 265–284, Springer, Berlin, Germany, 2008.
[36]
A. Casanueva, M. Tuffin, C. Cary, and D. A. Cowan, “Molecular adaptations to psychrophily: the impact of “omic” technologies,” Trends in Microbiology, vol. 18, no. 8, pp. 374–381, 2010.
[37]
N. F. W. Saunders, T. Thomas, P. M. G. Curmi et al., “Mechanisms of thermal adaptatation revealed from genomes of the anatarctic Archaea Methanogenium frigidum and Methanacoccoides burtonii,” Genome Research, vol. 13, no. 7, pp. 1580–1588, 2003.
[38]
R. Rabus, A. Ruepp, T. Frickey et al., “The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments,” Environmental Microbiology, vol. 6, no. 9, pp. 887–902, 2004.
[39]
C. Médigue, E. Krin, G. Pascal et al., “Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125,” Genome Research, vol. 15, no. 10, pp. 1325–1335, 2005.
[40]
B. A. Methé, K. E. Nelson, J. W. Deming et al., “The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 31, pp. 10913–10918, 2005.
[41]
E. Duchaud, M. Boussaha, V. Loux et al., “Complete genome sequence of the fish pathogen Flavobacterium psychrophilum,” Nature Biotechnology, vol. 25, no. 7, pp. 763–769, 2007.
[42]
M. Riley, J. T. Staley, A. Danchin et al., “Genomics of an extreme psychrophile, Psychromonas ingrahamii,” BMC Genomics, vol. 9, article 210, 2008.
[43]
D. F. Rodrigues, N. Ivanova, Z. He, M. Huebner, J. Zhou, and J. M. Tiedje, “Architecture of thermal adaptation in an Exiguobacterium sibiricum strain isolated from 3 million year old permafrost: a genome and transcriptome approach,” BMC Genomics, vol. 9, article 547, 2008.
[44]
M. A. Allen, F. M. Lauro, T. J. Williams et al., “The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation,” ISME Journal, vol. 3, no. 9, pp. 1012–1035, 2009.
[45]
H. L. Ayala-Del-Río, P. S. Chain, J. J. Grzymski et al., “The genome sequence of Psychrobacter arcticus 273-4, a psychroactive siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth,” Applied and Environmental Microbiology, vol. 76, no. 7, pp. 2304–2312, 2010.
[46]
C. Ng, M. Z. Demaere, T. J. Williams et al., “Metaproteogenomic analysis of a dominant green sulfur bacterium from Ace Lake, Antarctica,” ISME Journal, vol. 4, no. 8, pp. 1002–1019, 2010.
[47]
G. Blanc, I. Agarkova, J. Grimwood et al., “The genome of the polar eukaryotic microalga Coccomyxa subellipsoidea reveals traits of cold adaptation,” Genome Biology, vol. 13, article R39, 2012.
[48]
S. H. Jang, J. Kim, S. Hong, and C. Lee, “Genome sequence of cold-adapted Pseudomonas mandelii strain JR-1,” Journal of Bacteriology, vol. 194, p. 3263, 2012.
[49]
S. J. Kim, S. C. Shin, S. G. Hong et al., “Genome sequence of Janthinobacterium sp. strain PAMC, 25724, isolated from alpine glacier cryoconite,” Journal of Bacteriology, vol. 194, p. 2096, 2012.
[50]
A. Margolles, M. Gueimonde, and B. Sanchez, “Genome sequence of the antarctic psychrophile Bacterium Planococcus antarcticus DSM, 14505,” Journal of Bacteriology, vol. 194, p. 4465, 2012.
[51]
H. J. Park, S. C. Shin, and D. Kim, “Draft genome sequence of Arctic marine bacterium Pseudoalteromonas issachenkonii PAMC, 22718,” Journal of Bacteriology, vol. 194, p. 4140, 2012.
[52]
S. C. Shin, S. J. Kim, H. Ahn-do et al., “Genome sequence of a Salinibacterium sp. isolated from Antarctic soil,” Journal of Bacteriology, vol. 194, p. 2404, 2012.
[53]
S. C. Shin, S. J. Kim, S. G. Hong et al., “Genome sequence of Pseudomonas sp. strain PAMC, 25886, isolated from alpine glacial cryoconite,” Journal of Bacteriology, vol. 194, p. 1844, 2012.
[54]
P. M. Tribelli, L. J. R. Iustman, M. V. Catone et al., “Genome sequence of the polyhydroxybutyrate producer Pseudomonas extremaustralis, a highly stress-resistant Antarctic bacterium,” Journal of Bacteriology, vol. 194, pp. 2381–2382, 2012.
[55]
T. Watanabe, H. Kojima, and M. Fukui, “Draft genome sequence of a psychrotolerant sulfur-oxidizing bacterium, Sulfuricella denitrificans skB26, and proteomic insights into cold adaptation,” Applied and Environmental Microbiology, vol. 78, pp. 6545–6549, 2012.
[56]
G. Feller, “Molecular adaptations to cold in psychrophilic enzymes,” Cellular and Molecular Life Sciences, vol. 60, no. 4, pp. 648–662, 2003.
[57]
G. Feller and C. Gerday, “Psychrophilic enzymes: hot topics in cold adaptation,” Nature Reviews Microbiology, vol. 1, no. 3, pp. 200–208, 2003.
[58]
G. Feller, “Life at low temperatures: is disorder the driving force?” Extremophiles, vol. 11, no. 2, pp. 211–216, 2007.
[59]
G. Feller, “Enzyme function at low temperatures in Psychrophiles,” in Protein Adaptation in Extremophiles, K. S. Siddiqui and T. Thomas, Eds., pp. 35–69, Nova Science Publishers, New York, NY, USA, 2008.
[60]
G. Feller, “Protein stability and enzyme activity at extreme biological temperatures,” Journal of Physics: Condensed Matter, vol. 22, article 323101, 2010.
[61]
R. Margesin and G. Feller, “Biotechnological applications of psychrophiles,” Environmental Technology, vol. 31, no. 8-9, pp. 835–844, 2010.
[62]
F. Piette, C. Struvay, and G. Feller, “The protein folding challenge in psychrophiles: facts and current issues,” Environmental Microbiology, vol. 13, pp. 1924–1933, 2011.
[63]
F. Roulling, F. Piette, A. Cipolla, C. Struvay, and G. Feller, “Psychrophilic enzymes: cool responses to chilly problems,” in Extremophiles Handbook, K. Horikoshi, Ed., pp. 891–916, Springer, Berlin, Germany, 2011.
[64]
C. Struvay and G. Feller, “Optimization to low temperature activity in psychrophilic enzymes,” in International Journal of Molecular Sciences, vol. 13, pp. 11643–11665, 2012.
[65]
T. Araki, “Changes in rates of synthesis of individual proteins in a psychrophilic bacterium after a shift in temperature,” Canadian Journal of Microbiology, vol. 37, no. 11, pp. 840–847, 1991.
[66]
T. Araki, “The effect of temperature shifts on protein synthesis by the psychrophilic bacterium Vibrio sp. strain ANT-300,” Journal of General Microbiology, vol. 137, no. 4, pp. 817–826, 1991.
[67]
T. Araki, “An analysis of the effect of changes in growth temperature on proteolysis in vivo in the psychrophilic bacterium Vibrio sp. strain ANT-300,” Journal of General Microbiology, vol. 138, no. 10, pp. 2075–2082, 1992.
[68]
M. Hebraud, E. Dubois, P. Potier, and J. Labadie, “Effect of growth temperatures on the protein levels in a psychrotrophic bacterium, Pseudomonas fragi,” Journal of Bacteriology, vol. 176, no. 13, pp. 4017–4024, 1994.
[69]
M. Hébraud and P. Potier, “Cold shock response and low temperature adaptation in psychrotrophic bacteria,” Journal of Molecular Microbiology and Biotechnology, vol. 1, no. 2, pp. 211–219, 1999.
[70]
M. Hébraud and P. Potier, “Cold acclimation and cold shock response in psychrotrophic bacteria,” in Cold Shock, Response and Adaptation, M. Inouye and K. Yamanaka, Eds., pp. 41–60, Horizon Scientific Press, Norfolk, UK, 2000.
[71]
A. Goodchild, M. Raftery, N. F. W. Saunders, M. Guilhaus, and R. Cavicchioli, “Biology of the cold adapted archaeon, Methanococcoides burtonii determined by proteomics using liquid chromatography-tandem mass spectrometry,” Journal of Proteome Research, vol. 3, no. 6, pp. 1164–1176, 2004.
[72]
A. Goodchild, N. F. W. Saunders, H. Ertan et al., “A proteomic determination of cold adaptation in the Antarctic archaeon, Methanococcoides burtonii,” Molecular Microbiology, vol. 53, no. 1, pp. 309–321, 2004.
[73]
A. Goodchild, M. Raftery, N. F. W. Saunders, M. Guilliaus, and R. Cavicchioli, “Cold adaptation of the antarctic archaeon, Methanococcoides burtonii assessed by proteomics using ICAT,” Journal of Proteome Research, vol. 4, no. 2, pp. 473–480, 2005.
[74]
N. F. W. Saunders, A. Goodchild, M. Raftery, M. Guilhaus, P. M. G. Curmi, and R. Cavicchioli, “Predicted roles for hypothetical proteins in the low-temperature expressed proteome of the antarctic archaeon Methanococcoides burtonii,” Journal of Proteome Research, vol. 4, no. 2, pp. 464–472, 2005.
[75]
Y. Qiu, S. Kathariou, and D. M. Lubman, “Proteomic analysis of cold adaptation in a Siberian permafrost bacterium—Exiguobacterium sibiricum 255-15 by two-dimensional liquid separation coupled with mass spectrometry,” Proteomics, vol. 6, no. 19, pp. 5221–5233, 2006.
[76]
O. N. Reva, C. Weinel, M. Weinel et al., “Functional genomics of stress response in Pseudomonas putida KT2440,” Journal of Bacteriology, vol. 188, no. 11, pp. 4079–4092, 2006.
[77]
N. F. W. Saunders, C. Ng, M. Raftery, M. Guilhaus, A. Goodchild, and R. Cavicchioli, “Proteomic and computational analysis of secreted proteins with type I signal peptides from the antarctic archaeon Methanococcoides burtonii,” Journal of Proteome Research, vol. 5, no. 9, pp. 2457–2464, 2006.
[78]
C. Bakermans, S. L. Tollaksen, C. S. Giometti, C. Wilkerson, J. M. Tiedje, and M. F. Thomashow, “Proteomic analysis of Psychrobacter cryohalolentis K5 during growth at subzero temperatures,” Extremophiles, vol. 11, no. 2, pp. 343–354, 2007.
[79]
J. Kawamoto, T. Kurihara, M. Kitagawa, I. Kato, and N. Esaki, “Proteomic studies of an Antarctic cold-adapted bacterium, Shewanella livingstonensis Ac10, for global identification of cold-inducible proteins,” Extremophiles, vol. 11, no. 6, pp. 819–826, 2007.
[80]
S. Zheng, M. A. Ponder, J. Y. Shih, J. M. Tiedje, M. F. Thomashow, and D. M. Lubman, “A proteomic analysis of Psychrobacter articus 273-4 adaptation to low temperature and salinity using a 2-D liquid mapping approach,” Electrophoresis, vol. 28, no. 3, pp. 467–488, 2007.
[81]
P. W. Bergholz, C. Bakermans, and J. M. Tiedje, “Psychrobacter arcticus 273-4 Uses Resource Efficiency and Molecular Motion Adaptations for Subzero Temperature Growth,” Journal of Bacteriology, vol. 191, no. 7, pp. 2340–2352, 2009.
[82]
P. Wecker, C. Klockow, A. Ellrott et al., “Transcriptional response of the model planctomycete Rhodopirellula baltica SH1T to changing environmental conditions,” BMC Genomics, vol. 10, article no. 1471, p. 410, 2009.
[83]
F. Piette, S. D'Amico, C. Struvay et al., “Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125,” Molecular Microbiology, vol. 76, no. 1, pp. 120–132, 2010.
[84]
L. Ting, T. J. Williams, M. J. Cowley et al., “Cold adaptation in the marine bacterium, Sphingopyxis alaskensis, assessed using quantitative proteomics,” Environmental Microbiology, vol. 12, no. 10, pp. 2658–2676, 2010.
[85]
T. J. Williams, D. W. Burg, M. J. Raftery et al., “Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii part I: the effect of growth temperature,” Journal of Proteome Research, vol. 9, no. 2, pp. 640–652, 2010.
[86]
S. Campanaro, T. J. Williams, D. W. Burg et al., “Temperature-dependent global gene expression in the Antarctic archaeon Methanococcoides burtonii,” Environmental Microbiology, vol. 13, pp. 2018–2038, 2011.
[87]
N. C. S. Mykytczuk, J. T. Trevors, S. J. Foote, L. G. Leduc, G. D. Ferroni, and S. M. Twine, “Proteomic insights into cold adaptation of psychrotrophic and mesophilic Acidithiobacillus ferrooxidans strains,” Antonie van Leeuwenhoek, vol. 100, no. 2, pp. 259–277, 2011.
[88]
F. Piette, S. D'Amico, G. Mazzucchelli, A. Danchin, P. Leprince, and G. Feller, “Life in the cold: a proteomic study of cold-repressed proteins in the antarctic bacterium Pseudoalteromonas haloplanktis TAC125,” Applied and Environmental Microbiology, vol. 77, no. 11, pp. 3881–3883, 2011.
[89]
T. J. Williams, F. M. Lauro, H. Ertan et al., “Defining the response of a microorganism to temperatures that span its complete growth temperature range (-2°C to 28°C) using multiplex quantitative proteomics,” Environmental Microbiology, vol. 13, pp. 2186–2203, 2011.
[90]
M. V. Jagannadham and C. Chowdhury, “Differential expression of membrane proteins helps Antarctic Pseudomonas syringae to acclimatize upon temperature variations,” Journal of Proteomics, vol. 75, pp. 2488–2499, 2012.
[91]
J. Park, J. Kawamoto, N. Esaki, and T. Kurihara, “Identification of cold-inducible inner membrane proteins of the psychrotrophic bacterium, Shewanella livingstonensis Ac10, by proteomic analysis,” Extremophiles, vol. 16, pp. 227–236, 2012.
[92]
A. G. Pereira-Medrano, R. Margesin, and P. C. Wright, “Proteome characterization of the unsequenced psychrophile Pedobacter cryoconitis using metabolic labeling, tandem mass spectrometry, and a new bioinformatic workflow,” Proteomics, vol. 12, pp. 775–789, 2012.
[93]
F. Piette, P. Leprince, and G. Feller, “Is there a cold shock response in the Antarctic psychrophile Pseudoalteromonas haloplanktis?” Extremophiles, vol. 16, pp. 681–683, 2012.
[94]
F. Piette, C. Struvay, A. Godin, A. Cipolla, and G. Feller, “Life in the cold: proteomics of the Antarctic bacterium Pseudoalteromonas haloplanktis,” in Proteomic Applications in Biology, J. L. Heazlewood and C. J. Petzold, Eds., pp. 93–114, InTech, Rijeka, Croatia, 2012.
[95]
S. C. Shin, S. J. Kim, J. K. Lee et al., “Transcriptomics and comparative analysis of three antarctic notothenioid fishes,” PLoS One, vol. 7, article e43762, 2012.
[96]
Y. H. Jung, J. Y. Yi, H. J. Jung et al., “Overexpression of Cold shock protein A of Psychromonas arctica KOPRI 22215 confers cold-resistance,” Protein Journal, vol. 29, no. 2, pp. 136–142, 2010.
[97]
J. H. Uh, Y. H. Jung, Y. K. Lee, H. K. Lee, and H. Im, “Rescue of a cold-sensitive mutant at low temperatures by cold shock proteins from Polaribacter irgensii KOPRI 22228,” Journal of Microbiology, vol. 48, no. 6, pp. 798–802, 2010.
[98]
J. Lim, T. Thomas, and R. Cavicchioli, “Low temperature regulated DEAD-box RNA helicase from the Antarctic archaeon, Methanococcoides burtonii,” Journal of Molecular Biology, vol. 297, no. 3, pp. 553–567, 2000.
[99]
G. Cartier, F. Lorieux, F. Allemand, M. Dreyfus, and T. Bizebard, “Cold adaptation in DEAD-box proteins,” Biochemistry, vol. 49, no. 12, pp. 2636–2646, 2010.
[100]
K. Yoshimune, A. Galkin, L. Kulakova, T. Yoshimura, and N. Esaki, “Cold-active DnaK of an Antarctic psychrotroph Shewanella sp. Ac10 supporting the growth of dnaK-null mutant of Escherichia coli at cold temperatures,” Extremophiles, vol. 9, no. 2, pp. 145–150, 2005.
[101]
M. Sung, H. Im, and K. Lee, “Molecular cloning and chaperone activity of DnaK from cold-adapted bacteria, KOPRI22215,” Bulletin of the Korean Chemical Society, vol. 32, no. 6, pp. 1925–1930, 2011.
[102]
M. Ferrer, T. N. Chernikova, M. M. Yakimov, P. N. Golyshin, and K. N. Timmis, “Chaperonins govern growth of Escherichia coli at low temperatures,” Nature Biotechnology, vol. 21, no. 11, pp. 1266–1267, 2003.
[103]
M. Ferrer, H. Lünsdorf, T. N. Chernikova, M. Yakimov, K. N. Timmis, and P. N. Golyshin, “Functional consequences of single:double ring transitions in chaperonins: life in the cold,” Molecular Microbiology, vol. 53, no. 1, pp. 167–182, 2004.
[104]
M. Strocchi, M. Ferrer, K. N. Timmis, and P. N. Golyshin, “Low temperature-induced systems failure in Escherichia coli: insights from rescue by cold-adapted chaperones,” Proteomics, vol. 6, no. 1, pp. 193–206, 2006.
[105]
F. U. Hartl and M. Hayer-Hartl, “Converging concepts of protein folding in vitro and in vivo,” Nature Structural and Molecular Biology, vol. 16, no. 6, pp. 574–581, 2009.
[106]
O. Kandror and A. L. Goldberg, “Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 10, pp. 4978–4981, 1997.
[107]
R. L. Baldwin, “The search for folding intermediates and the mechanism of protein folding,” Annual Review of Biophysics, vol. 37, pp. 1–21, 2008.
[108]
K. S. Siddiqui and R. Cavicchioli, “Cold-adapted enzymes,” Annual Review of Biochemistry, vol. 75, pp. 403–433, 2006.
[109]
Y. Suzuki, M. Haruki, K. Takano, M. Morikawa, and S. Kanaya, “Possible involvement of an FKBP family member protein from a psychrotrophic bacterium Shewanella sp. SIB1 in cold-adaptation,” European Journal of Biochemistry, vol. 271, no. 7, pp. 1372–1381, 2004.
[110]
G. Zoldák, T. Aumüller, C. Lücke et al., “A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases,” Biochemistry, vol. 48, no. 43, pp. 10423–10436, 2009.
[111]
K. A. Luke, C. L. Higgins, and P. Wittung-Stafshede, “Thermodynamic stability and folding of proteins from hyperthermophilic organisms,” FEBS Journal, vol. 274, no. 16, pp. 4023–4033, 2007.
[112]
A. Mukaiyama and K. Takano, “Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding,” International Journal of Molecular Sciences, vol. 10, no. 3, pp. 1369–1385, 2009.
[113]
J. Okada, T. Okamoto, A. Mukaiyama et al., “Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins,” BMC Evolutionary Biology, vol. 10, no. 1, article 207, 2010.
[114]
A. Cipolla, S. D'Amico, R. Barumandzadeh, A. Matagne, and G. Feller, “Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic alpha-amylase from Antarctic Bacterium,” The Journal of Biological Chemistry, vol. 286, pp. 38348–38355, 2011.
[115]
T. Collins, M. Matzapetakis, and H. Santos, “Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125,” Biomolecular NMR Assignments, vol. 4, no. 2, pp. 151–154, 2010.
[116]
N. Aghajari, G. Feller, C. Gerday, and R. Haser, “Structures of the psychrophilic Alteromonas haloplanctisα-amylase give insights into cold adaptation at a molecular level,” Structure, vol. 6, no. 12, pp. 1503–1516, 1998.
[117]
N. Aghajari, G. Feller, C. Gerday, and R. Haser, “Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor,” Protein Science, vol. 7, no. 3, pp. 564–572, 1998.
[118]
F. Van Petegem, T. Collins, M. A. Meuwis, C. Gerday, G. Feller, and J. Van Beeumen, “The structure of a cold-adapted family 8 xylanase at 1.3 ？ resolution. Structural adaptations to cold and investigation of the active site,” Journal of Biological Chemistry, vol. 278, no. 9, pp. 7531–7539, 2003.
[119]
S. Violot, N. Aghajari, M. Czjzek et al., “Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering,” Journal of Molecular Biology, vol. 348, no. 5, pp. 1211–1224, 2005.
[120]
A. Merlino, I. R. Krauss, I. Castellano et al., “Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis,” Journal of Structural Biology, vol. 172, no. 3, pp. 343–352, 2010.
[121]
V. Alterio, V. Aurilia, A. Romanelli et al., “Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125,” Biopolymers, vol. 93, no. 8, pp. 669–677, 2010.
[122]
N. Aghajari, F. Van Petegem, V. Villeret et al., “Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases,” Proteins, vol. 50, no. 4, pp. 636–647, 2003.
[123]
C. Michaux, J. Massant, F. Kerff et al., “Crystal structure of a cold-adapted class C β-lactamase,” FEBS Journal, vol. 275, no. 8, pp. 1687–1697, 2008.
[124]
R. J. M. Russell, U. Gerike, M. J. Danson, D. W. Hough, and G. L. Taylor, “Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium,” Structure, vol. 6, no. 3, pp. 351–362, 1998.
[125]
T. Skalova, J. Dohnalek, V. Spiwok et al., “Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1. 9 ？ resolution,” Journal of Molecular Biology, vol. 353, pp. 282–294, 2005.
[126]
O. Almog, A. González, N. Godin et al., “The crystal structures of the psychrophilic subtilisin S41 and the mesophilic subtilisin Sph reveal the same calcium-loaded state,” Proteins, vol. 74, no. 2, pp. 489–496, 2009.
[127]
A. J. M. Nel, I. M. Tuffin, B. T. Sewell, and D. A. Cowan, “Unique aliphatic amidase from a psychrotrophic and haloalkaliphilic Nesterenkonia isolate,” Applied and Environmental Microbiology, vol. 77, no. 11, pp. 3696–3702, 2011.
[128]
E. Wang, D. Koutsioulis, H. K. S. Leiros et al., “Crystal Structure of Alkaline Phosphatase from the Antarctic Bacterium TAB5,” Journal of Molecular Biology, vol. 366, no. 4, pp. 1318–1331, 2007.
[129]
C. Bauvois, L. Jacquamet, A. L. Huston, F. Borel, G. Feller, and J. L. Ferrer, “Crystal structure of the cold-active aminopeptidase from Colwellia psychrerythraea, a close structural homologue of the human bifunctional leukotriene A4 hydrolase,” Journal of Biological Chemistry, vol. 283, no. 34, pp. 23315–23325, 2008.
[130]
H. K. S. Leiros, A. L. Pey, M. Innselset et al., “Structure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stability,” Journal of Biological Chemistry, vol. 282, no. 30, pp. 21973–21986, 2007.
[131]
S. Y. Kim, K. Y. Hwang, S. H. Kim, H. C. Sung, Y. S. Han, and Y. Cho, “Structural basis for cold adaptation: sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum,” Journal of Biological Chemistry, vol. 274, no. 17, pp. 11761–11767, 1999.
[132]
J. Arnórsdóttir, M. M. Kristjánsson, and R. Ficner, “Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation,” FEBS Journal, vol. 272, no. 3, pp. 832–845, 2005.
[133]
A. E. Fed？y, N. Yang, A. Martinez, H. K. S. Leiros, and I. H. Steen, “Structural and Functional Properties of Isocitrate Dehydrogenase from the Psychrophilic Bacterium Desulfotalea psychrophila Reveal a Cold-active Enzyme with an Unusual High Thermal Stability,” Journal of Molecular Biology, vol. 372, no. 1, pp. 130–149, 2007.
[134]
D. De Vos, Y. Xu, P. Hulpiau, B. Vergauwen, and J. J. Van Beeumen, “Structural investigation of cold activity and regulation of aspartate carbamoyltransferase from the extreme psychrophilic bacterium Moritella profunda,” Journal of Molecular Biology, vol. 365, no. 2, pp. 379–395, 2007.
[135]
E. Bae and G. N. Phillips Jr., “Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases,” Journal of Biological Chemistry, vol. 279, no. 27, pp. 28202–28208, 2004.
[136]
M. Davlieva and Y. Shamoo, “Structure and biochemical characterization of an adenylate kinase originating from the psychrophilic organism Marinibacillus marinus,” Acta Crystallographica F, vol. 65, no. 8, pp. 751–756, 2009.
[137]
M. Alvarez, J. P. Zeelen, V. Mainfroid et al., “Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus: kinetic and structural properties,” Journal of Biological Chemistry, vol. 273, no. 4, pp. 2199–2206, 1998.
[138]
S. C. Zhang, M. Sun, T. Li et al., “Structure analysis of a new psychrophilic marine protease,” PLoS One, vol. 6, article e26939, 2011.
[139]
H. Tsuruta, B. Mikami, and Y. Aizono, “Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp,” Journal of Biochemistry, vol. 137, no. 1, pp. 69–77, 2005.
[140]
E. K. Riise, M. S. Lorentzen, R. Helland, A. O. Smal？s, H. K. S. Leiros, and N. P. Willassen, “The first structure of a cold-active catalase from Vibrio salmonicida at 1.96 ？ reveals structural aspects of cold adaptation,” Acta Crystallographica D, vol. 63, no. 2, pp. 135–148, 2007.
[141]
B. Altermark, R. Helland, E. Moe, N. P. Willassen, and A. O. Smal？s, “Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida,” Acta Crystallographica D, vol. 64, no. 4, pp. 368–376, 2008.
[142]
S. K. Jung, D. G. Jeong, M. S. Lee et al., “Structural basis for the cold adaptation of psychrophilic M37 lipase from Photobacterium lipolyticum,” Proteins, vol. 71, no. 1, pp. 476–484, 2008.
[143]
H. L. Pedersen, N. P. Willassen, and I. Leiros, “The first structure of a cold-adapted superoxide dismutase (SOD): biochemical and structural characterization of iron SOD from Aliivibrio salmonicida,” Acta Crystallographica F, vol. 65, no. 2, pp. 84–92, 2009.
[144]
R. Helland, R. L. Larsen, and B. ásgeirsson, “The 1.4？ crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase,” Biochimica et Biophysica Acta, vol. 1794, no. 2, pp. 297–308, 2009.
[145]
H. Tsuruta, B. Mikami, T. Higashi, and Y. Aizono, “Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp,” Bioscience, Biotechnology and Biochemistry, vol. 74, no. 1, pp. 69–74, 2010.
[146]
M. De Backer, S. McSweeney, H. B. Rasmussen, B. W. Riise, P. Lindley, and E. Hough, “The 1.9 ？ crystal structure of heat-labile shrimp alkaline phosphatase,” Journal of Molecular Biology, vol. 318, no. 5, pp. 1265–1274, 2002.
[147]
N. Coquelle, E. Fioravanti, M. Weik, F. Vellieux, and D. Madern, “Activity, Stability and Structural Studies of Lactate Dehydrogenases Adapted to Extreme Thermal Environments,” Journal of Molecular Biology, vol. 374, no. 2, pp. 547–562, 2007.
[148]
A. O. Smalas, E. S. Heimstad, A. Hordvik, N. P. Willassen, and R. Male, “Cold adaption of enzymes: structural comparison between salmon and bovine trypsins,” Proteins, vol. 20, no. 2, pp. 149–166, 1994.
[149]
G. I. Berglund, N. P. Willassen, A. Hordvik, and A. O. Smalas, “Structure of native pancreatic elastase from North Atlantic salmon at 1.61 Angstrom resolution,” Acta Crystallographica D, vol. 51, no. 6, pp. 925–937, 1995.
[150]
S. Karlsen, E. Hough, and R. L. Olsen, “Structure and proposed amino-acid sequence of a pepsin from Atlantic cod (Gadus morhua),” Acta Crystallographica D, vol. 54, no. 1, pp. 32–46, 1998.
[151]
I. Leiros, E. Moe, O. Lanes, A. O. Smal？s, and N. P. Willassen, “The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features,” Acta Crystallographica D, vol. 59, no. 8, pp. 1357–1365, 2003.
[152]
M. E. Peterson, R. Eisenthal, M. J. Danson, A. Spence, and R. M. Daniel, “A new intrinsic thermal parameter for enzymes reveals true temperature optima,” Journal of Biological Chemistry, vol. 279, pp. 20717–20722, 2004.
[153]
C. K. Lee, R. M. Daniel, C. Shepherd et al., “Eurythermalism and the temperature dependence of enzyme activity,” FASEB Journal, vol. 21, no. 8, pp. 1934–1941, 2007.
[154]
M. E. Peterson, R. M. Daniel, M. J. Danson, and R. Eisenthal, “The dependence of enzyme activity on temperature: determination and validation of parameters,” Biochemical Journal, vol. 402, no. 2, pp. 331–337, 2007.
[155]
T. Collins, F. Roulling, F. Piette et al., “Fundamentals of cold-adapted enzymes,” in Psychrophiles, from Biodiversity to Biotechnology, R. Margesin, F. Schinner, J. C. Marx, and C. Gerday, Eds., pp. 211–227, Springer, Berlin, Germany, 2008.
[156]
G. Feller, T. Lonhienne, C. Deroanne, C. Libioulle, J. Van Beeumen, and C. Gerday, “Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23,” Journal of Biological Chemistry, vol. 267, no. 8, pp. 5217–5221, 1992.
[157]
S. Davail, G. Feller, E. Narinx, and C. Gerday, “Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus TA41,” Journal of Biological Chemistry, vol. 269, no. 26, pp. 17448–17453, 1994.
[158]
D. Georlette, B. Damien, V. Blaise et al., “Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases,” Journal of Biological Chemistry, vol. 278, no. 39, pp. 37015–37023, 2003.
[159]
T. Collins, M. A. Meuwis, C. Gerday, and G. Feller, “Activity, stability and flexibility in glycosidases adapted to extreme thermal environments,” Journal of Molecular Biology, vol. 328, no. 2, pp. 419–428, 2003.
[160]
S. D'Amico, J. C. Marx, C. Gerday, and G. Feller, “Activity-stability relationships in extremophilic enzymes,” Journal of Biological Chemistry, vol. 278, no. 10, pp. 7891–7896, 2003.
[161]
K. S. Siddiqui, G. Feller, S. D'Amico, C. Gerday, L. Giaquinto, and R. Cavicchioli, “The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted α-amylase,” Journal of Bacteriology, vol. 187, no. 17, pp. 6197–6205, 2005.
[162]
P. A. Fields and G. N. Somero, “Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 19, pp. 11476–11481, 1998.
[163]
T. Lonhienne, C. Gerday, and G. Feller, “Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility,” Biochimica et Biophysica Acta, vol. 1543, no. 1, pp. 1–10, 2000.
[164]
R. Chiuri, G. Maiorano, A. Rizzello et al., “Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases,” Biophysical Journal, vol. 96, no. 4, pp. 1586–1596, 2009.
[165]
T. Lonhienne, J. Zoidakis, C. E. Vorgias, G. Feller, C. Gerday, and V. Bouriotis, “Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic antarctic bacterium,” Journal of Molecular Biology, vol. 310, no. 2, pp. 291–297, 2001.
[166]
P. Claverie, C. Vigano, J. M. Ruysschaert, C. Gerday, and G. Feller, “The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation,” Biochimica et Biophysica Acta, vol. 1649, no. 2, pp. 119–122, 2003.
[167]
Y. Suzuki, K. Takano, and S. Kanaya, “Stabilities and activities of the N- and C-domains of FKBP22 from a psychrotrophic bacterium overproduced in Escherichia coli,” FEBS Journal, vol. 272, no. 3, pp. 632–642, 2005.
[168]
M. Qian, R. Haser, G. Buisson, E. Duee, and F. Payan, “The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-？ resolution,” Biochemistry, vol. 33, no. 20, pp. 6284–6294, 1994.
[169]
N. Aghajari, M. Roth, and R. Haser, “Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic α-amylase,” Biochemistry, vol. 41, no. 13, pp. 4273–4280, 2002.
[170]
S. Bjelic, B. O. Brandsdal, and J. ？qvist, “Cold adaptation of enzyme reaction rates,” Biochemistry, vol. 47, no. 38, pp. 10049–10057, 2008.
[171]
D. De Vos, T. Collins, W. Nerinckx et al., “Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the β-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product,” Biochemistry, vol. 45, no. 15, pp. 4797–4807, 2006.
[172]
M. Olufsen, A. O. Smal？s, and B. O. Brandsdal, “Electrostatic interactions play an essential role in DNA repair and cold-adaptation of Uracil DNA glycosylase,” Journal of Molecular Modeling, vol. 14, no. 3, pp. 201–213, 2008.
[173]
I. L. U. Raeder, E. Moe, N. P. Willassen, A. O. Smal？s, and I. Leiros, “Structure of uracil-DNA N-glycosylase (UNG) from Vibrio cholerae: mapping temperature adaptation through structural and mutational analysis,” Acta Crystallographica F, vol. 66, no. 2, pp. 130–136, 2010.
[174]
E. Papaleo, M. Olufsen, L. De Gioia, and B. O. Brandsdal, “Optimization of electrostatics as a strategy for cold-adaptation: a case study of cold- and warm-active elastases,” Journal of Molecular Graphics and Modelling, vol. 26, no. 1, pp. 93–103, 2007.
[175]
A. A. Gorfe, B. O. Brandsdal, H. K. S. Leiros, R. Helland, and A. O. Smal？s, “Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: qualitative evaluation of electrostatic differences at the substrate binding site,” Proteins, vol. 40, no. 2, pp. 207–217, 2000.
[176]
A. O. Smal？s, H. K. Leiros, V. Os, and N. P. Willassen, “Cold adapted enzymes,” Biotechnology Annual Review, vol. 6, pp. 1–57, 2000.
[177]
B. O. Brandsdal, A. O. Smal？s, and J. ？qvist, “Electrostatic effects play a central role in cold adaptation of trypsin,” FEBS Letters, vol. 499, no. 1-2, pp. 171–175, 2001.
[178]
E. Moe, I. Leiros, E. K. Riise et al., “Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG) from Atlantic cod (Gadus morhua),” Journal of Molecular Biology, vol. 343, no. 5, pp. 1221–1230, 2004.
[179]
G. Garsoux, J. Lamotte, C. Gerday, and G. Feller, “Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis,” Biochemical Journal, vol. 384, no. 2, pp. 247–253, 2004.
[180]
I. Tsigos, K. Velonia, I. Smonou, and V. Bouriotis, “Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123,” European Journal of Biochemistry, vol. 254, no. 2, pp. 356–362, 1998.
[181]
S. D'Amico, J. S. Sohier, and G. Feller, “Kinetics and energetics of ligand binding determined by microcalorimetry: insights into active site mobility in a psychrophilic α-amylase,” Journal of Molecular Biology, vol. 358, no. 5, pp. 1296–1304, 2006.
[182]
K. Sun, L. Camardella, G. Di Prisco, and G. Hervé, “Properties of aspartate transcarbamylase from TAD1, a psychrophilic bacterial strain isolated from Antarctica,” FEMS Microbiology Letters, vol. 164, no. 2, pp. 375–382, 1998.
[183]
Y. Xu, Y. Zhang, Z. Liang, M. Van De Casteele, C. Legrain, and N. Glansdorff, “Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, Vibrio strain 2693: properties of the enzyme, genetic organization and synthesis in Escherichia coli,” Microbiology, vol. 144, no. 5, pp. 1435–1441, 1998.
[184]
E. Narinx, E. Baise, and C. Gerday, “Subtilisin from psychrophilic antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold,” Protein Engineering, vol. 10, no. 11, pp. 1271–1279, 1997.
[185]
D. Georlette, Z. O. Jónsson, F. Van Petegem et al., “A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures,” European Journal of Biochemistry, vol. 267, no. 12, pp. 3502–3512, 2000.
[186]
M. Masullo, P. Arcari, B. De Paola, A. Parmeggiani, and V. Bocchini, “Psychrophilic elongation factor Tu from the antarctic Moraxella sp. Tac II 25: biochemical characterization and cloning of the encoding gene,” Biochemistry, vol. 39, no. 50, pp. 15531–15539, 2000.
[187]
M. A. Ciardiello, L. Camardella, V. Carratore, and G. Di Prisco, “L-Glutamate dehydrogenase from the Antarctic fish Chaenocephalus aceratus: primary structure, function and thermodynamic characterisation: relationship with cold adaptation,” Biochimica et Biophysica Acta, vol. 1543, no. 1, pp. 11–23, 2000.
[188]
R. Di Fraia, V. Wilquet, M. A. Ciardiello et al., “NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant bacterium Psychrobacter sp. TAD1: characterization, protein and DNA sequence, and relationship to other glutamate dehydrogenases,” European Journal of Biochemistry, vol. 267, no. 1, pp. 121–131, 2000.
[189]
S. D'Amico, C. Gerday, and G. Feller, “Structural Determinants of Cold Adaptation and Stability in a Large Protein,” Journal of Biological Chemistry, vol. 276, no. 28, pp. 25791–25796, 2001.
[190]
Y. Xu, G. Feller, C. Gerday, and N. Glansdorff, “Moritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature?” Journal of Bacteriology, vol. 185, no. 18, pp. 5519–5526, 2003.
[191]
R. M. Evans, E. M. Behiry, L. H. Tey, J. Guo, E. J. Loveridge, and R. K. Allemann, “Catalysis by dihydrofolate reductase from the psychropiezophile Moritella profunda,” ChemBioChem, vol. 11, no. 14, pp. 2010–2017, 2010.
[192]
B. Altermark, L. Niiranen, N. P. Willassen, A. O. Smal？s, and E. Moe, “Comparative studies of endonuclease I from cold-adapted Vibrio salmonicida and mesophilic Vibrio cholerae,” FEBS Journal, vol. 274, no. 1, pp. 252–263, 2007.
[193]
L. Birolo, L. M. Tutino, B. Fontanella et al., “Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling,” European Journal of Biochemistry, vol. 267, no. 9, pp. 2790–2802, 2000.
[194]
S. Watanabe, Y. Yasutake, I. Tanaka, and Y. Takada, “Elucidation of stability determinants of cold-adapted monomeric isocitrate dehydrogenase from a psychrophilic bacterium, Colwellia maris, by construction of chimeric enzymes,” Microbiology, vol. 151, no. 4, pp. 1083–1094, 2005.
[195]
T. Collins, M. A. Meuwis, I. Stals, M. Claeyssens, G. Feller, and C. Gerday, “A novel family 8 xylanase, functional and physicochemical characterization,” Journal of Biological Chemistry, vol. 277, no. 38, pp. 35133–35139, 2002.
[196]
Y. Xu, G. Feller, C. Gerday, and N. Glansdorff, “Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi,” Journal of Bacteriology, vol. 185, no. 7, pp. 2161–2168, 2003.
[197]
U. Gerike, M. J. Danson, N. J. Russell, and D. W. Hough, “Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R,” European Journal of Biochemistry, vol. 248, no. 1, pp. 49–57, 1997.
[198]
X. Li, X. Jiang, H. Li, and D. Ren, “Purine nucleoside phosphorylase from Pseudoalteromonas sp. Bsi590: molecular cloning, gene expression and characterization of the recombinant protein,” Extremophiles, vol. 12, no. 3, pp. 325–333, 2008.
[199]
M. A. Tang, H. Motoshima, and K. Watanabe, “Fluorescence studies on the stability, flexibility and substrate-induced conformational changes of acetate kinases from psychrophilic and mesophilic bacteria,” The Protein Journal, vol. 31, pp. 337–344, 2012.
[200]
B. ásgeirsson and P. Cekan, “Microscopic rate-constants for substrate binding and acylation in cold-adaptation of trypsin I from Atlantic cod,” FEBS Letters, vol. 580, no. 19, pp. 4639–4644, 2006.
[201]
P. S. Low, J. L. Bada, and G. N. Somero, “Temperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 70, no. 2, pp. 430–432, 1973.
[202]
G. Feller and C. Gerday, “Psychrophilic enzymes: molecular basis of cold adaptation,” Cellular and Molecular Life Sciences, vol. 53, no. 10, pp. 830–841, 1997.
[203]
T. Thomas and R. Cavicchioli, “Effect of temperature on stability and activity of elongation factor 2 proteins from Antarctic and thermophilic methanogens,” Journal of Bacteriology, vol. 182, no. 5, pp. 1328–1332, 2000.
[204]
A. Hoyoux, I. Jennes, P. Dubois et al., “Cold-Adapted β-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas haloplanktis,” Applied and Environmental Microbiology, vol. 67, no. 4, pp. 1529–1535, 2001.
[205]
S. Y. Lam, R. C. Y. Yeung, T. H. Yu, K. H. Sze, and K. B. Wong, “A rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity,” PLoS Biology, vol. 9, no. 3, Article ID e1001027, 2011.
[206]
F. R. Gurd and T. M. Rothgeb, “Motions in proteins,” Advances in Protein Chemistry, vol. 33, pp. 73–165, 1979.
[207]
K. A. Henzler-Wildman, M. Lei, V. Thai, S. J. Kerns, M. Karplus, and D. Kern, “A hierarchy of timescales in protein dynamics is linked to enzyme catalysis,” Nature, vol. 450, no. 7171, pp. 913–916, 2007.
[208]
A. J. Baldwin and L. E. Kay, “NMR spectroscopy brings invisible protein states into focus,” Nature Chemical Biology, vol. 5, no. 11, pp. 808–814, 2009.
[209]
P. L. Privalov, “Stability of proteins. Proteins which do not present a single cooperative system,” Advances in Protein Chemistry, vol. 35, pp. 1–104, 1982.
[210]
P. Závodszky, J. Kardos, A. Svingor, and G. A. Petsko, “Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 13, pp. 7406–7411, 1998.
[211]
P. A. Fields, “Protein function at thermal extremes: balancing stability and flexibility,” Comparative Biochemistry and Physiology A, vol. 129, pp. 417–431, 2001.
[212]
O. Shlyk-Kerner, I. Samish, D. Kaftan et al., “Protein flexibility acclimatizes photosynthetic energy conversion to the ambient temperature,” Nature, vol. 442, no. 7104, pp. 827–830, 2006.
[213]
M. Tehei, B. Franzetti, D. Madern et al., “Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering,” EMBO Reports, vol. 5, no. 1, pp. 66–70, 2004.
[214]
M. Tehei and G. Zaccai, “Adaptation to extreme environments: macromolecular dynamics in complex systems,” Biochimica et Biophysica Acta, vol. 1724, no. 3, pp. 404–410, 2005.
[215]
G. N. Somero, “Proteins and temperature,” Annual Review of Physiology, vol. 57, pp. 43–68, 1995.
[216]
A. L. Huston, J. Z. Haeggstr？m, and G. Feller, “Cold adaptation of enzymes: structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile Colwellia psychrerythraea and of human leukotriene A4 hydrolase,” Biochimica et Biophysica Acta, vol. 1784, no. 11, pp. 1865–1872, 2008.
[217]
M. Bentahir, G. Feller, M. Aittaleb et al., “Structural, kinetic, and calorimetric characterization of the cold- active phosphoglycerate kinase from the antarctic Pseudomonas sp. TACII18,” Journal of Biological Chemistry, vol. 275, no. 15, pp. 11147–11153, 2000.
[218]
Z. X. Liang, I. Tsigos, T. Lee et al., “Evidence for increased local flexibility in psychrophilic alcohol dehydrogenase relative to its thermophilic homologue,” Biochemistry, vol. 43, no. 46, pp. 14676–14683, 2004.
[219]
P. A. Fields, B. D. Wahlstrand, and G. N. Somero, “Intrinsic versus extrinsic stabilization of enzymes: the interaction of solutes and temperature on A4-lactate dehydrogenase orthologs from warm-adapted and cold-adapted marine fishes,” European Journal of Biochemistry, vol. 268, no. 16, pp. 4497–4505, 2001.
[220]
A. Svingor, J. Kardos, I. Hajdú, A. Németh, and P. Závodszky, “A better enzyme to cope with cold: comparative flexibility studies on psychrotrophic, mesophilic, and thermophilic IPMDHs,” Journal of Biological Chemistry, vol. 276, no. 30, pp. 28121–28125, 2001.
[221]
Z. X. Liang, I. Tsigos, V. Bouriotis, and J. P. Klinman, “Impact of protein flexibility on hydride-transfer parameters in thermophilic and psychrophilic alcohol dehydrogenases,” Journal of the American Chemical Society, vol. 126, pp. 9500–9501, 2004.
[222]
M. Olufsen, A. O. Smal？s, E. Moe, and B. O. Brandsdal, “Increased flexibility as a strategy for cold adaptation: a comparative molecular dynamics study of cold- and warm-active uracil DNA glycosylase,” Journal of Biological Chemistry, vol. 280, no. 18, pp. 18042–18048, 2005.
[223]
E. S. Heimstad, L. K. Hansen, and A. O. Smalas, “Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution,” Protein Engineering, vol. 8, no. 4, pp. 379–388, 1995.
[224]
B. O. Brandsdal, E. S. Heimstad, I. Sylte, and A. O. Smal？s, “Comparative molecular dynamics of mesophilic and psychrophilic protein homologues studied by 1.2 ns simulations,” Journal of Biomolecular Structure and Dynamics, vol. 17, no. 3, pp. 493–506, 1999.
[225]
O. A. Adekoya, R. Helland, N. P. Willassen, and I. Sylte, “Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family,” Proteins, vol. 62, no. 2, pp. 435–449, 2006.
[226]
E. Papaleo, L. Riccardi, C. Villa, P. Fantucci, and L. De Gioia, “Flexibility and enzymatic cold-adaptation: a comparative molecular dynamics investigation of the elastase family,” Biochimica et Biophysica Acta, vol. 1764, no. 8, pp. 1397–1406, 2006.
[227]
V. Spiwok, P. Lipovova, T. Skalova et al., “Cold-active enzymes studied by comparative molecular dynamics simulation,” Journal of Molecular Modeling, vol. 13, pp. 485–497, 2007.
[228]
E. Papaleo, M. Pasi, L. Riccardi, I. Sambi, P. Fantucci, and L. D. Gioia, “Protein flexibility in psychrophilic and mesophilic trypsins. Evidence of evolutionary conservation of protein dynamics in trypsin-like serine-proteases,” FEBS Letters, vol. 582, no. 6, pp. 1008–1018, 2008.
[229]
V. Aurilia, J. F. Rioux-Dubé, A. Marabotti, M. Pézolet, and S. D'Auria, “Structure and dynamics of cold-adapted enzymes as investigated by FT-IR spectroscopy and MD. the case of an esterase from Pseudoalteromonas haloplanktis,” Journal of Physical Chemistry B, vol. 113, no. 22, pp. 7753–7761, 2009.
[230]
M. Pasi, L. Riccardi, P. Fantucci, L. De Gioia, and E. Papaleo, “Dynamic properties of a psychrophilic α-amylase in comparison with a mesophilic homologue,” Journal of Physical Chemistry B, vol. 113, no. 41, pp. 13585–13595, 2009.
[231]
E. Papaleo, M. Tiberti, G. Invernizzi, M. Pasi, and V. Ranzani, “Molecular determinants of enzyme cold adaptation: comparative structural and computational studies of cold- and warm-adapted enzymes,” Current Protein and Peptide Science, vol. 12, pp. 657–683, 2011.
[232]
M. Tiberti and E. Papaleo, “Dynamic properties of extremophilic subtilisin-like serine-proteases,” Journal of Structural Biology, vol. 174, no. 1, pp. 69–83, 2011.
[233]
G. Feller, D. D'Amico, and C. Gerday, “Thermodynamic stability of a cold-active α-amylase from the antarctic bacterium Alteromonas haloplanctis,” Biochemistry, vol. 38, no. 14, pp. 4613–4619, 1999.
[234]
S. D'Amico, C. Gerday, and G. Feller, “Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted α-amylase,” Journal of Biological Chemistry, vol. 277, no. 48, pp. 46110–46115, 2002.
[235]
W. J. Becktel and J. A. Schellman, “Protein stability curves,” Biopolymers, vol. 26, no. 11, pp. 1859–1877, 1987.
[236]
P. L. Privalov, “Stability of proteins small globular proteins,” Advances in Protein Chemistry, vol. 33, pp. 167–241, 1979.
[237]
P. L. Privalov, “Cold denaturation of proteins,” Critical Reviews in Biochemistry and Molecular Biology, vol. 25, pp. 281–305, 1990.
[238]
S. Kumar and R. Nussinov, “Experiment-guided thermodynamic simulations on reversible two-state proteins: implications for protein thermostability,” Biophysical Chemistry, vol. 111, no. 3, pp. 235–246, 2004.
[239]
D. C. Rees and A. D. Robertson, “Some thermodynamic implications for the thermostability of proteins,” Protein Science, vol. 10, no. 6, pp. 1187–1194, 2001.
[240]
S. Kumar, C. J. Tsai, and R. Nussinov, “Maximal stabilities of reversible two-state proteins,” Biochemistry, vol. 41, no. 17, pp. 5359–5374, 2002.
[241]
O. García-Arribas, R. Mateo, M. M. Tomczak, P. L. Davies, and M. G. Mateu, “Thermodynamic stability of a cold-adapted protein, type III antifreeze protein, and energetic contribution of salt bridges,” Protein Science, vol. 16, no. 2, pp. 227–238, 2007.
[242]
G. I. Makhatadze and P. L. Privalov, “Energetics of protein structure,” Advances in Protein Chemistry, vol. 47, pp. 307–425, 1995.
[243]
P. A. Sigala, D. A. Kraut, J. M. M. Caaveiro et al., “Testing geometrical discrimination within an enzyme active site: constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole,” Journal of the American Chemical Society, vol. 130, no. 41, pp. 13696–13708, 2008.
[244]
N. J. Russell, “Toward a molecular understanding of cold activity of enzymes from psychrophiles,” Extremophiles, vol. 4, no. 2, pp. 83–90, 2000.
[245]
G. Gianese, F. Bossa, and S. Pascarella, “Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes,” Proteins, vol. 47, no. 2, pp. 236–249, 2002.
[246]
R. A. Goldstein, “Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: insights from the quasi-chemical approximation,” Protein Science, vol. 16, no. 9, pp. 1887–1895, 2007.
[247]
C. Alimenti, A. Vallesi, B. Pedrini, K. Wüthrich, and P. Luporini, “Molecular cold-adaptation: comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes,” IUBMB Life, vol. 61, no. 8, pp. 838–845, 2009.
[248]
K. Mavromatis, I. Tsigos, M. Tzanodaskalaki, M. Kokkinidis, and V. Bouriotis, “Exploring the role of a glycine cluster in cold adaptation of an alkaline phosphatase,” European Journal of Biochemistry, vol. 269, no. 9, pp. 2330–2335, 2002.
[249]
L. Kulakova, A. Galkin, T. Nakayama, T. Nishino, and N. Esaki, “Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly→Pro substitution near the active site on its catalytic activity and stability,” Biochimica et Biophysica Acta, vol. 1696, no. 1, pp. 59–65, 2004.
[250]
M. Sakaguchi, M. Matsuzaki, K. Niimiya, J. Seino, Y. Sugahara, and M. Kawakita, “Role of proline residues in conferring thermostability on aqualysin I,” Journal of Biochemistry, vol. 141, no. 2, pp. 213–220, 2007.
[251]
K. S. Siddiqui, A. Poljak, M. Guilhaus et al., “Role of lysine versus arginine in enzyme cold-adaptation: modifying lysine to homo-arginine stabilizes the cold-adapted α-amylase from Pseudoalteromonas haloplanktis,” Proteins, vol. 64, no. 2, pp. 486–501, 2006.
[252]
B. B. Xie, F. Bian, X. L. Chen et al., “Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics: new insights into relationship between conformational flexibility and hydrogen bonding,” Journal of Biological Chemistry, vol. 284, no. 14, pp. 9257–9269, 2009.
[253]
G. S？lensminde, J. O. Halskau Jr., and I. Jonassen, “Amino acid contacts in proteins adapted to different temperatures: hydrophobic interactions and surface charges play a key role,” Extremophiles, vol. 13, no. 1, pp. 11–20, 2009.
[254]
D. I. Paredes, K. Watters, D. J. Pitman, C. Bystroff, and J. S. Dordick, “Comparative void-volume analysis of psychrophilic and mesophilic enzymes: structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility,” BMC Structural Biology, vol. 11, article 42, 2011.
[255]
F. Rentier-Delrue, S. C. Mande, S. Moyens et al., “Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences,” Journal of Molecular Biology, vol. 229, no. 1, pp. 85–93, 1993.
[256]
G. Feller, Z. Zekhnini, J. Lamotte-Brasseur, and C. Gerday, “Enzymes from cold-adapted microorganisms. The class C β-lactamase from the antarctic psychrophile Psychrobacter immobilis A5,” European Journal of Biochemistry, vol. 244, no. 1, pp. 186–191, 1997.
[257]
G. Feller, F. Payan, F. Theys, M. Qian, R. Haser, and C. Gerday, “Stability and structural analysis of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23,” European Journal of Biochemistry, vol. 222, no. 2, pp. 441–447, 1994.
[258]
K. S. Siddiqui, A. Poljak, M. Guilhaus et al., “Role of disulfide bridges in the activity and stability of a cold-active α-amylase,” Journal of Bacteriology, vol. 187, no. 17, pp. 6206–6212, 2005.
[259]
K. S. P. Yip, T. J. Stillman, K. L. Britton et al., “The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures,” Structure, vol. 3, no. 11, pp. 1147–1158, 1995.
[260]
C. Vetriani, D. L. Maeder, N. Tolliday et al., “Protein thermostability above 100°C: a key role for ionic interactions,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 21, pp. 12300–12305, 1998.
[261]
G. S. Bell, R. J. M. Russell, H. Connaris, D. W. Hough, M. J. Danson, and G. L. Taylor, “Stepwise adaptations of citrate synthase to survival at life's extremes: from psychrophile to hyperthermophile,” European Journal of Biochemistry, vol. 269, no. 24, pp. 6250–6260, 2002.
[262]
L. Mandrich, M. Pezzullo, P. Del Vecchio, G. Barone, M. Rossi, and G. Manco, “Analysis of thermal adaptation in the HSL enzyme family,” Journal of Molecular Biology, vol. 335, no. 1, pp. 357–369, 2004.
[263]
B. Altermark, S. Thorvaldsen, E. Moe, A. O. Smal？s, and N. P. Willassen, “Sequence comparison and environmental adaptation of a bacterial endonuclease,” Computational Biology and Chemistry, vol. 31, no. 3, pp. 163–172, 2007.
[264]
S. Thorvaldsen, E. Hjerde, C. Fenton, and N. P. Willassen, “Molecular characterization of cold adaptation based on ortholog protein sequences from Vibrionaceae species,” Extremophiles, vol. 11, no. 5, pp. 719–732, 2007.
[265]
D. Tronelli, E. Maugini, F. Bossa, and S. Pascarella, “Structural adaptation to low temperatures—analysis of the subunit interface of oligomeric psychrophilic enzymes,” FEBS Journal, vol. 274, no. 17, pp. 4595–4608, 2007.
[266]
B. Zheng, W. Yang, X. Zhao et al., “Crystal structure of hyperthermophilic endo-beta-1, 4-glucanase: implications for catalytic mechanism and thermostability,” The Journal of Biological Chemistry, vol. 287, pp. 8336–8346, 2012.
[267]
E. De Vendittis, I. Castellano, R. Cotugno, M. R. Ruocco, G. Raimo, and M. Masullo, “Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition,” Journal of Theoretical Biology, vol. 250, no. 1, pp. 156–171, 2008.
[268]
G. S？lensminde, J. O. Halskau Jr., R. Helland, N. P. Willassen, and I. Jonassen, “Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins,” Extremophiles, vol. 11, no. 4, pp. 585–596, 2007.
[269]
M. Jahandideh, S. M. H. Barkooie, S. Jahandideh et al., “Elucidating the protein cold-adaptation: investigation of the parameters enhancing protein psychrophilicity,” Journal of Theoretical Biology, vol. 255, no. 1, pp. 113–118, 2008.
[270]
M. T. H. Khan and I. Sylte, “Determinants for psychrophilic and thermophilic features of metallopeptidases of the M4 family,” In Silico Biology, vol. 9, no. 3, pp. 105–124, 2009.
[271]
R. P. R. Metpally and B. V. B. Reddy, “Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: insights into the molecular basis of cold adaptation of proteins,” BMC Genomics, vol. 10, article 11, 2009.
[272]
N. Aghajari, G. Feller, C. Gerday, and R. Haser, “Structural basis of α-amylase activation by chloride,” Protein Science, vol. 11, no. 6, pp. 1435–1441, 2002.
[273]
S. D'Amico, C. Gerday, and G. Feller, “Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted α-amylase,” Journal of Molecular Biology, vol. 332, no. 5, pp. 981–988, 2003.
[274]
E. Papaleo, M. Pasi, M. Tiberti, and L. De Gioia, “Molecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutations,” PLoS One, vol. 6, article e24214, 2011.
[275]
H. Laurell, J. A. Contreras, I. Castan, D. Langin, and C. Holm, “Analysis of the psychrotolerant property of hormone-sensitive lipase through site-directed mutagenesis,” Protein Engineering, vol. 13, no. 10, pp. 711–717, 2000.
[276]
U. Gerike, M. J. Danson, and D. W. Hough, “Cold-active citrate synthase: mutagenesis of active-site residues,” Protein Engineering, vol. 14, no. 9, pp. 655–661, 2001.
[277]
N. Ohtani, M. Haruki, M. Morikawa, and S. Kanaya, “Heat labile ribonuclease HI from a psychrotrophic bacterium: gene cloning, characterization and site-directed mutagenesis,” Protein Engineering, vol. 14, no. 12, pp. 975–982, 2001.
[278]
I. Tsigos, K. Mavromatis, M. Tzanodaskalaki, C. Pozidis, M. Kokkinidis, and V. Bouriotis, “Engineering the properties of a cold active enzyme through rational redesign of the active site,” European Journal of Biochemistry, vol. 268, no. 19, pp. 5074–5080, 2001.
[279]
K. Mavromatis, G. Feller, M. Kokkinidis, and V. Bouriotis, “Cold adaptation of a psychrophilic chitinase: a mutagenesis study,” Protein Engineering, vol. 16, no. 7, pp. 497–503, 2003.
[280]
J. Arnórsdóttir, S. Helgadóttir, S. H. Thorbjarnardóttir, G. Eggertsson, and M. M. Kristjánsson, “Effect of selected Ser/Ala and Xaa/Pro mutations on the stability and catalytic properties of a cold adapted subtilisin-like serine proteinase,” Biochimica et Biophysica Acta, vol. 1774, no. 6, pp. 749–755, 2007.
[281]
Y. R. Yang, H. Zhu, N. Fang et al., “Cold-adapted maturation of thermophilic WF146 protease by mimicking the propeptide binding interactions of psychrophilic subtilisin S41,” FEBS Letters, vol. 582, no. 17, pp. 2620–2626, 2008.
[282]
S. Matsuo, H. Shirai, and Y. Takada, “Isocitrate dehydrogenase isozymes from a psychrotrophic bacterium, Pseudomonas psychrophila,” Archives of Microbiology, vol. 192, no. 8, pp. 639–650, 2010.
[283]
K. Miyazaki, P. L. Wintrode, R. A. Grayling, D. N. Rubingh, and F. H. Arnold, “Directed evolution study of temperature adaptation in a psychrophilic enzyme,” Journal of Molecular Biology, vol. 297, no. 4, pp. 1015–1026, 2000.
[284]
P. L. Wintrode, K. Miyazaki, and F. H. Arnold, “Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution,” Journal of Biological Chemistry, vol. 275, no. 41, pp. 31635–31640, 2000.
[285]
E. Bae and G. N. Phillips Jr., “Roles of static and dynamic domains in stability and catalysis of adenylate kinase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 7, pp. 2132–2137, 2006.
[286]
P. L. Wintrode and F. H. Arnold, “Temperature adaptation of enzymes: lessons from laboratory evolution,” Advances in Protein Chemistry, vol. 55, pp. 161–225, 2000.
[287]
S. D'Amico, P. Claverie, T. Collins et al., “Molecular basis of cold adaptation,” Philosophical Transactions of the Royal Society B, vol. 357, no. 1423, pp. 917–925, 2002.
[288]
L. Giver, A. Gershenson, P. O. Freskgard, and F. H. Arnold, “Directed evolution of a thermostable esterase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 22, pp. 12809–12813, 1998.
[289]
J. R. Cherry, M. H. Lamsa, P. Schneider et al., “Directed evolution of a fungal peroxidase,” Nature Biotechnology, vol. 17, no. 4, pp. 379–384, 1999.
[290]
A. Noguchi, T. Nishino, and T. Nakayama, “Kinetic and thermodynamic characterization of the cold activity acquired upon single amino-acid substitution near the active site of a thermostable α-glucosidase,” Journal of Molecular Catalysis B, vol. 56, no. 4, pp. 300–306, 2009.
[291]
A. Tosco, L. Birolo, S. Madonna, G. Lolli, G. Sannia, and G. Marino, “GroEL from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125: molecular characterization and gene cloning,” Extremophiles, vol. 7, no. 1, pp. 17–28, 2003.
[292]
R. Cotugno, M. Ruocco, S. Marco et al., “Differential cold-adaptation among protein components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125,” Molecular BioSystems, vol. 5, no. 5, pp. 519–528, 2009.
[293]
P. Falasca, G. Evangelista, R. Cotugno et al., “Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125,” Extremophiles, vol. 16, pp. 539–552, 2012.
[294]
A. R. Dinner, A. ？alib, L. J. Smitha, C. M. Dobsona, and M. Karplus, “Understanding protein folding via free-energy surfaces from theory and experiment,” Trends in Biochemical Sciences, vol. 25, no. 7, pp. 331–339, 2000.
[295]
C. P. Schultz, “Illuminating folding intermediates,” Nature Structural & Molecular Biology, vol. 7, pp. 7–10, 2000.
[296]
C. J. Tsai, B. Ma, and R. Nussinov, “Folding and binding cascades: shifts in energy landscapes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 18, pp. 9970–9972, 1999.
[297]
S. Kumar, B. Ma, C. J. Tsai, N. Sinha, and R. Nussinov, “Folding and binding cascades: dynamic landscapes and population shifts,” Protein Science, vol. 9, no. 1, pp. 10–19, 2000.
[298]
B. Ma, S. Kumar, C. J. Tsai, Z. Hu, and R. Nussinov, “Transition-state ensemble in enzyme catalysis: possibility, reality, or necessity?” Journal of Theoretical Biology, vol. 203, no. 4, pp. 383–397, 2000.
[299]
S. J. Benkovic, G. G. Hammes, and S. Hammes-Schiffer, “Free-energy landscape of enzyme catalysis,” Biochemistry, vol. 47, no. 11, pp. 3317–3321, 2008.
[300]
S. Bandi and B. E. Bowler, “Probing the bottom of a folding funnel using conformationally gated electron transfer reactions,” Journal of the American Chemical Society, vol. 130, no. 24, pp. 7540–7541, 2008.
[301]
T. P. Schrank, D. W. Bolen, and V. J. Hilser, “Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 40, pp. 16984–16989, 2009.
[302]
P. Mereghetti, L. Riccardi, B. O. Brandsdal, P. Fantucci, L. De Gioia, and E. Papaleo, “Near native-state conformational landscape of psychrophilic and mesophilic enzymes: probing the folding funnel model,” Journal of Physical Chemistry B, vol. 114, no. 22, pp. 7609–7619, 2010.
[303]
R. Margesin and F. Schinner, Biotechnological Applications of Cold-Adapted Organisms, Springer, Heidelberg, Germany, 1999.
[304]
C. Gerday, M. Aittaleb, M. Bentahir et al., “Cold-adapted enzymes: from fundamentals to biotechnology,” Trends in Biotechnology, vol. 18, no. 3, pp. 103–107, 2000.
[305]
D. Allen, A. L. Huston, L. E. Weels, and J. W. Deming, “Biotechnological use of psychrophiles,” in Encyclopedia of Environmental Microbiology, G. Bitton, Ed., pp. 1–17, John Wiley & Sons, New York, NY, USA, 2002.
[306]
R. Cavicchioli, K. S. Siddiqui, D. Andrews, and K. R. Sowers, “Low-temperature extremophiles and their applications,” Current Opinion in Biotechnology, vol. 13, no. 3, pp. 253–261, 2002.
[307]
J. C. Marx, T. Collins, S. D'Amico, G. Feller, and C. Gerday, “Cold-adapted enzymes from marine Antarctic microorganisms,” Marine Biotechnology, vol. 9, no. 3, pp. 293–304, 2007.
[308]
R. Cavicchioli, T. Charlton, H. Ertan, S. M. Omar, K. S. Siddiqui, and T. J. Williams, “Biotechnological uses of enzymes from psychrophiles,” Microbial Biotechnology, vol. 4, no. 4, pp. 449–460, 2011.
[309]
H. Kobori, C. W. Sullivan, and H. Shizuya, “Heat-labile alkaline phosphatase from Antarctic bacteria: rapid 5' end-labeling of nucleic acids,” Proceedings of the National Academy of Sciences of the United States of America, vol. 81, no. 21, pp. 6691–6695, 1984.
[310]
M. Rina, C. Pozidis, K. Mavromatis, M. Tzanodaskalaki, M. Kokkinidis, and V. Bouriotis, “Alkaline phosphatase from the Antarctic strain TAB5 properties and psychrophilic adaptations,” European Journal of Biochemistry, vol. 267, no. 4, pp. 1230–1238, 2000.
[311]
D. Koutsioulis, E. Wang, M. Tzanodaskalaki et al., “Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase,” Protein Engineering, Design and Selection, vol. 21, no. 5, pp. 319–327, 2008.
[312]
J. Babu, P. W. Ramteke, and G. Thomas, “Cold active microbial lipases: some hot issues and recent developments,” Biotechnology Advances, vol. 26, no. 5, pp. 457–470, 2008.
[313]
D. Lohan and S. Johnston, “UNU-IAS report: bioprospecting in Antarctica,” http://www.ias.unu.edu/binaries2/antarctic_bioprospecting.pdf.
[314]
T. Collins, D. De Vos, A. Hoyoux et al., “Study of the active site residues of a glycoside hydrolase family 8 xylanase,” Journal of Molecular Biology, vol. 354, no. 2, pp. 425–435, 2005.
[315]
T. Collins, A. Hoyoux, A. Dutron et al., “Use of glycoside hydrolase family 8 xylanases in baking,” Journal of Cereal Science, vol. 43, no. 1, pp. 79–84, 2006.
[316]
E. Dornez, P. Verjans, F. Arnaut, J. A. Delcour, and C. M. Courtin, “Use of psychrophilic xylanases provides insight into the xylanase functionality in bread making,” Journal of Agricultural and Food Chemistry, vol. 59, pp. 9553–9562, 2011.
[317]
K. S. Siddiqui, A. Poljak, and R. Cavicchioli, “Improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives,” Cellular and Molecular Biology, vol. 50, no. 5, pp. 657–667, 2004.
[318]
K. S. Siddiqui and R. Cavicchioli, “Improved thermal stability and activity in the cold-adapted lipase B from Candida antarctica following chemical modification with oxidized polysaccharides,” Extremophiles, vol. 9, no. 6, pp. 471–476, 2005.
[319]
K. S. Siddiqui, D. M. Parkin, P. M. G. Curmi et al., “A novel approach for enhancing the catalytic efficiency of a protease at low temperature: reduction in substrate inhibition by chemical modification,” Biotechnology and Bioengineering, vol. 103, no. 4, pp. 676–686, 2009.
[320]
C. Smal, M. Aran, E. Lanzarotti, et al., “1H, 15N and 13C chemical shift assignments of the BA42 protein of the psychrophilic bacteria Bizionia argentinensis sp. nov,” Biomolecular NMR Assignments, vol. 6, no. 2, pp. 181–183, 2012.
