biostudies-literatureDu HMinistry of Science and Technology of the People's Republic of ChinaNational Natural Science Foundation of Chinae00110https://www.ebi.ac.uk/biostudies/studies/S-EPMC6508853biostudies-literatureUnknown3(2)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 gPlant directA new insight to explore the regulation between S-nitrosylation and N-glycosylation.PMC65088532014CB9434023152100131830017Zhan NZuo JMu JChen LDu HRen BfalseA new insight to explore the regulation between S-nitrosylation and N-glycosylation.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 g2019-01-01T00:00:00Z2019 Feb2026-07-14T13:39:56.124Z2019-07-25T07:15:46ZS-EPMC65088533124575810.1002/pld3.110