%0 Journal Article
%T A new insight to explore the regulation between Sİ\nitrosylation and Nİ\glycosylation
%A Bo Ren
%A Hu Du
%A Jianru Zuo
%A Jinye Mu
%A Lichao Chen
%A Ni Zhan
%J Archive of "Plant Direct".
%D 2019
%R 10.1002/pld3.110
%X Nitric oxide (NO) is a signal molecule in plants and animals. Arabidopsis GSNO reductase1 (AtGSNOR1) catalyzes metabolism of Sİ\nitrosoglutathione (GSNO) which is a major biologically active NO species. The GSNOR1 lossİ\ofİ\function mutant gsnor1İ\3 overaccumulates GSNO with inherent high Sİ\nitrosylation level and resistance to the oxidative stress inducer paraquat (1,1Ħäİ\dimethylİ\4,4Ħäİ\bipyridinium dichloride). Here, we report the characterization of dgl1İ\3 as a genetic suppressor of gsnor1İ\3. DGL1 encodes a subunit of the oligosaccharyltransferse (OST) complex which catalyzes the formation of Nİ\glycosidic bonds in Nİ\glycosylation. The fact that dgl1İ\3 repressed the paraquat resistance of gsnor1İ\3 meanwhile gsnor1İ\3 rescued the embryoİ\lethal and postİ\embryonic development defect of dgl1İ\3 reminded us the possibility that Sİ\nitrosylation and Nİ\glycosylation crosstalk with each other through coİ\substrates. By enriching glycoproteins in gsnor1İ\3 and mass spectrometry analysis, TGG2 (thioglucoside glucohydrolase2) was identified as one of coİ\substrates with high degradation rate and elevated Nİ\glycosylation level in gsnor1İ\3 ost3/6. The Sİ\nitrosylation and Nİ\glycosylation profiles were also modified in dgl1İ\3 and gsnor1İ\3. Thereby, we propose a linkage between Sİ\nitrosylation and Nİ\glycosylation through coİ\substrates
%K Arabidopsis
%K DGL1
%K gsnor1İ\3
%K Nİ\glycosylation
%K Sİ\nitrosylation
%K TGG2
%U https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6508853/