%0 Journal Article
%T A new insight to explore the regulation between S-nitrosylation and N-glycosylation.
%A Du H
%A Chen L
%A Zhan N
%A Mu J
%A Ren B
%A Zuo J
%J Plant Direct
%V 3
%N 2
%D Feb 2019
%M 31245758
%F 3.369
%R 10.1002/pld3.110
%X Nitric oxide (NO) is a signal molecule in plants and animals. Arabidopsis GSNO reductase1 (AtGSNOR1) catalyzes metabolism of S-nitrosoglutathione (GSNO) which is a major biologically active NO species. The GSNOR1 loss-of-function mutant gsnor1-3 overaccumulates GSNO with inherent high S-nitrosylation level and resistance to the oxidative stress inducer paraquat (1,1'-dimethyl-4,4'-bipyridinium dichloride). Here, we report the characterization of dgl1-3 as a genetic suppressor of gsnor1-3. DGL1 encodes a subunit of the oligosaccharyltransferse (OST) complex which catalyzes the formation of N-glycosidic bonds in N-glycosylation. The fact that dgl1-3 repressed the paraquat resistance of gsnor1-3 meanwhile gsnor1-3 rescued the embryo-lethal and post-embryonic development defect of dgl1-3 reminded us the possibility that S-nitrosylation and N-glycosylation crosstalk with each other through co-substrates. By enriching glycoproteins in gsnor1-3 and mass spectrometry analysis, TGG2 (thioglucoside glucohydrolase2) was identified as one of co-substrates with high degradation rate and elevated N-glycosylation level in gsnor1-3 ost3/6. The S-nitrosylation and N-glycosylation profiles were also modified in dgl1-3 and gsnor1-3. Thereby, we propose a linkage between S-nitrosylation and N-glycosylation through co-substrates.