ShanghaiTech University Knowledge Management System
| Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions | |
| 2015-10-23 | |
| Source Publication | JOURNAL OF BIOLOGICAL CHEMISTRY
 |
| ISSN | 0021-9258 |
| Volume | 290Issue:43Pages:26314-26327 |
| Status | 已发表 |
| DOI | 10.1074/jbc.M115.681999 |
| Abstract | 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. |
| Indexed By | SCI ; EI |
| Language | 英语 |
| Funding Project | Committee of Science and Technology in Shanghai Grant[12JC1409700] |
| WOS Research Area | Biochemistry & Molecular Biology |
| WOS Subject | Biochemistry & Molecular Biology |
| WOS ID | WOS:000363527300047 |
| Publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| EI Accession Number | 20154401452793 |
| EI Keywords | Amino acids ; Cytology ; Scaffolds (biology) |
| EI Classification Number | Bioengineering and Biology:461 ; Organic Compounds:804.1 |
| WOS Keyword | ESCHERICHIA-COLI ; MESSENGER-RNA ; P43 COMPONENT ; TRANSLATION ; AUTOPHAGY ; ACTIVATION ; EXPRESSION ; APOPTOSIS ; MTOR ; DIFFERENTIATION |
| Original Document Type | Article |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/2106 |
| Collection | 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 |
| Corresponding Author | Wang, En-Duo |
| Affiliation | 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 |
| Corresponding Author Affilication | School of Life Science and Technology |
| Recommended Citation 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. |
| Files in This Item: | Download All | |||||
| File Name/Size | DocType | Version | Access | License | ||
Edit Comment
Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.