Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions

doi:10.1074/jbc.M115.681999

	Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions
	Lei, Hui-Yan 1,2; Zhou, Xiao-Long 1,2; Ruan, Zhi-Rong 1,2; Sun, Wei-Cheng1,2,3 ; Eriani, Gilbert 4; Wang, En-Duo1,2,3
	2015-10-23
发表期刊	JOURNAL OF BIOLOGICAL CHEMISTRY (IF:4.0[JCR-2023],4.4[5-Year])
ISSN	0021-9258
卷号	290 期号:43 页码:26314-26327
发表状态	已发表
DOI	10.1074/jbc.M115.681999
摘要	Nine aminoacyl-tRNA synthetases (aaRSs) and three scaffold proteins form a super multiple aminoacyl-tRNA synthetase complex (MSC) in the human cytoplasm. Domains that have been added progressively to MSC components during evolution are linked by unstructured flexible peptides, producing an elongated and multiarmed MSC structure that is easily attacked by proteases in vivo. A yeast two-hybrid screen for proteins interacting with LeuRS, a representative MSC member, identified calpain 2, a calcium-activated neutral cysteine protease. Calpain 2 and calpain 1 could partially hydrolyze most MSC components to generate specific fragments that resembled those reported previously. The cleavage sites of calpain in ArgRS, GlnRS, and p43 were precisely mapped. After cleavage, their N-terminal regions were removed. Sixty-three amino acid residues were removed from the N terminus of ArgRS to form ArgRS Delta N63; GlnRS formed GlnRS Delta N198, and p43 formed p43 Delta N106. GlnRS Delta N198 had a much weaker affinity for its substrates, tRNA(Gln) and glutamine. p43 Delta N106 was the same as the previously reported p43-derived apoptosis-released factor. The formation of p43 Delta N106 by calpain depended on Ca2+ and could be specifically inhibited by calpeptin and by RNAi of the regulatory subunit of calpain in vivo. These results showed, for the first time, that calpain plays an essential role in dissociating the MSC and might regulate the canonical and non-canonical functions of certain components of the MSC.
收录类别	SCI ; EI
语种	英语
资助项目	Committee of Science and Technology in Shanghai Grant[12JC1409700]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000363527300047
出版者	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
EI入藏号	20154401452793
EI主题词	Amino acids ; Cytology ; Scaffolds (biology)
EI分类号	Bioengineering and Biology:461 ; Organic Compounds:804.1
WOS关键词	ESCHERICHIA-COLI ; MESSENGER-RNA ; P43 COMPONENT ; TRANSLATION ; AUTOPHAGY ; ACTIVATION ; EXPRESSION ; APOPTOSIS ; MTOR ; DIFFERENTIATION
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/2106
专题	生命科学与技术学院生命科学与技术学院_特聘教授组_王恩多组生命科学与技术学院_硕士生
通讯作者	Wang, En-Duo
作者单位	1.Chinese Acad Sci, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci, State Key Lab Mol Biol, Shanghai 200031, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100039, Peoples R China 3.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 200031, Peoples R China 4.Univ Strasbourg, CNRS, Inst Biol Mol & Cellulaire, Architecture & Reactivite ARN,UPR9002, F-67084 Strasbourg, France
通讯作者单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Lei, Hui-Yan,Zhou, Xiao-Long,Ruan, Zhi-Rong,et al. Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2015,290(43):26314-26327.
APA	Lei, Hui-Yan,Zhou, Xiao-Long,Ruan, Zhi-Rong,Sun, Wei-Cheng,Eriani, Gilbert,&Wang, En-Duo.(2015).Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions.JOURNAL OF BIOLOGICAL CHEMISTRY,290(43),26314-26327.
MLA	Lei, Hui-Yan,et al."Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions".JOURNAL OF BIOLOGICAL CHEMISTRY 290.43(2015):26314-26327.