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Site-Specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis

文献类型：期刊论文

作者Hu, Jiliang3,5; Huang, Xiahe2; Chen, Lichao3,5; Sun, Xuwu1; Lu, Congming1; Zhang, Lixin1; Wang, Yingchun2; Zuo, Jianru3
刊名PLANT PHYSIOLOGY
出版日期2015
卷号167期号:4页码:1731-1746
ISSN号0032-0889
DOI10.1104/pp.15.00026
文献子类Article
英文摘要Nitric oxide (NO) regulates multiple developmental events and stress responses in plants. A major biologically active species of NO is S-nitrosoglutathione (GSNO), which is irreversibly degraded by GSNO reductase (GSNOR). The major physiological effect of NO is protein S-nitrosylation, a redox-based posttranslational modification mechanism by covalently linking an NO molecule to a cysteine thiol. However, little is known about the mechanisms of S-nitrosylation-regulated signaling, partly due to limited S-nitrosylated proteins being identified. In this study, we identified 1,195 endogenously S-nitrosylated peptides in 926 proteins from the Arabidopsis (Arabidopsis thaliana) by a site-specific nitrosoproteomic approach, which, to date, is the largest data set of S-nitrosylated proteins among all organisms. Consensus sequence analysis of these peptides identified several motifs that contain acidic, but not basic, amino acid residues flanking the S-nitrosylated cysteine residues. These S-nitrosylated proteins are involved in a wide range of biological processes and are significantly enriched in chlorophyll metabolism, photosynthesis, carbohydrate metabolism, and stress responses. Consistently, the gsnor1-3 mutant shows the decreased chlorophyll content and altered photosynthetic properties, suggesting that S-nitrosylation is an important regulatory mechanism in these processes. These results have provided valuable resources and new clues to the studies on S-nitrosylation-regulated signaling in plants.
学科主题Plant Sciences
出版地CARY
电子版国际标准刊号1532-2548
WOS关键词LIGHT-HARVESTING COMPLEX ; CHLOROPHYLL-B SYNTHESIS ; NITRIC-OXIDE ; CELL-DEATH ; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE ; NITROSOGLUTATHIONE REDUCTASE ; PROTEOMIC ANALYSIS ; PHOTOSYSTEM-II ; PLANT-GROWTH ; GLUTATHIONE
WOS研究方向Science Citation Index Expanded (SCI-EXPANDED)
语种英语
WOS记录号WOS:000354438500041
出版者OXFORD UNIV PRESS INC
资助机构National Natural Science Foundation of China [91217302, 31130014] ; State Key Laboratory of Plant Genomics [2011B0525-02]
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/25658]  
专题中科院光生物学重点实验室
作者单位1.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
2.Chinese Acad Sci, Natl Plant Gene Res Ctr, Beijing 100101, Peoples R China
3.Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Plant Genom, Beijing 100101, Peoples R China
4.Chinese Acad Sci, Inst Bot, Beijing 100093, Peoples R China
5.Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Mol Dev Biol, Beijing 100101, Peoples R China
推荐引用方式
GB/T 7714		 Hu, Jiliang,Huang, Xiahe,Chen, Lichao,et al. Site-Specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis[J]. PLANT PHYSIOLOGY,2015,167(4):1731-1746.
APA Hu, Jiliang.,Huang, Xiahe.,Chen, Lichao.,Sun, Xuwu.,Lu, Congming.,...&Zuo, Jianru.(2015).Site-Specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis.PLANT PHYSIOLOGY,167(4),1731-1746.
MLA Hu, Jiliang,et al."Site-Specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis".PLANT PHYSIOLOGY 167.4(2015):1731-1746.

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来源：植物研究所

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