文献类型: 外文期刊
作者: Du, Hu 1 ; Chen, Lichao 2 ; Zhan, Ni 2 ; Mu, Jinye 2 ; Ren, Bo 2 ; Zuo, Jianru 2 ;
作者机构: 1.Guangdong Acad Agr Sci, Vegetable Res Inst, Guangdong Key Lab New Technol Res Vegetables, Guangzhou, Peoples R China
2.Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Plant Genom, Beijing, Peoples R China
3.Chinese Acad Sci, Inst Genet & Dev Biol, Natl Plant Gene Res Ctr Beijing, Beijing, Peoples R China
4.Univ Chinese Acad Sci, Beijing, Peoples R China
关键词: Arabidopsis; DGL1; gsnor1-3; N-glycosylation; S-nitrosylation; TGG2
期刊名称:PLANT DIRECT ( 影响因子:3.038; 五年影响因子:3.017 )
ISSN:
年卷期: 2019 年 3 卷 2 期
页码:
收录情况: SCI
摘要: 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.
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