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

doi:10.1104/pp.15.00026

IB-CAS > 中科院光生物学重点实验室

	Site-Specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis
	Hu, Jiliang 1,3; Huang, Xiahe 2; Chen, Lichao 1,3; Sun, Xuwu 4; Lu, Congming 4; Zhang, Lixin4 ; Wang, Yingchun 2; Zuo, Jianru 1
	2015
发表期刊	PLANT PHYSIOLOGY
ISSN	0032-0889
卷号	167 期号:4 页码:1731-1746
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.
学科领域	Plant Sciences
DOI	10.1104/pp.15.00026
收录类别	SCI
语种	英语
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)
WOS记录号	WOS:000354438500041
出版者	OXFORD UNIV PRESS INC
文献子类	Article
出版地	CARY
EISSN	1532-2548
资助机构	National Natural Science Foundation of China [91217302, 31130014] ; State Key Laboratory of Plant Genomics [2011B0525-02]
作者邮箱	jrzuo@genetics.ac.cn
作品OA属性	Bronze, Green Published
引用统计	被引频次：165[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	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, Inst Genet & Dev Biol, State Key Lab Plant Genom, Beijing 100101, 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 Mol Dev Biol, Beijing 100101, Peoples R China 4.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 5.Chinese Acad Sci, Inst Bot, Beijing 100093, 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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