Newly acquired N-terminal extension targets threonyl-tRNA synthetase-like protein into the multiple tRNA synthetase complex

doi:10.1093/nar/gkz588

	Newly acquired N-terminal extension targets threonyl-tRNA synthetase-like protein into the multiple tRNA synthetase complex
	Zhou, Xiao-Long 1; Chen, Yun 1; Zeng, Qi-Yu 1; Ruan, Zhi-Rong 1; Fang, Pengfei 2; Wang, En-Duo1,3
	2019-09-19
发表期刊	NUCLEIC ACIDS RESEARCH
ISSN	0305-1048
卷号	47 期号:16 页码:8662-8674
发表状态	已发表
DOI	10.1093/nar/gkz588
摘要	A typical feature of eukaryotic aminoacyl-tRNA synthetases (aaRSs) is the evolutionary gain of domains at either the N- or C-terminus, which frequently mediating protein-protein interaction. TARSL2 (mouse Tarsl2), encoding a threonyl-tRNA synthetase-like protein (ThrRS-L), is a recently identified aaRS-duplicated gene in higher eukaryotes, with canonical functions in vitro, which exhibits a different N-terminal extension (N-extension) from TARS (encoding ThrRS). We found the first half of the N-extension of human ThrRS-L (hThrRS-L) is homologous to that of human arginyl-tRNA synthetase. Using the N-extension as a probe in a yeast two-hybrid screening, AIMP1/p43 was identified as an interactor with hThrRS-L. We showed that ThrRS-L is a novel component of the mammalian multiple tRNA synthetase complex (MSC), and is reliant on two leucine zippers in the N-extension for MSC-incorporation in humans, and mouse cell lines and muscle tissue. The N-extension was sufficient to target a foreign protein into the MSC. The results from a Tarsl2-deleted cell line showed that it does not mediate MSC integrity. The effect of phosphorylation at various sites of hThrRS-L on its MSC-targeting is also explored. In summary, we revealed that ThrRS-L is a bona fide component of the MSC, which is mediated by a newly evolved N-extension domain.
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收录类别	SCI ; SCIE
语种	英语
资助项目	Youth Innovation Promotion Association (Chinese Academy of Sciences)[Y119S41291]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000490576900030
出版者	OXFORD UNIV PRESS
WOS关键词	AMINOACYL-TRANSFER-RNA ; 2 FORMS ; TRANSLATION ; COMPONENTS
原始文献类型	Article
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/80386
专题	生命科学与技术学院_特聘教授组_王恩多组
通讯作者	Zhou, Xiao-Long; Wang, En-Duo
作者单位	1.Univ Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, Chinese Acad Sci, State Key Lab Mol Biol,CAS Ctr Excellence Mol Cel, 320 Yue Yang Rd, Shanghai 200031, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Organ Chem, Ctr Excellence Mol Synth, State Key Lab Bioorgan & Nat Prod Chem, 345 Lingling Rd, Shanghai 200032, Peoples R China 3.ShanghaiTech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai 201210, Peoples R China
通讯作者单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Zhou, Xiao-Long,Chen, Yun,Zeng, Qi-Yu,et al. Newly acquired N-terminal extension targets threonyl-tRNA synthetase-like protein into the multiple tRNA synthetase complex[J]. NUCLEIC ACIDS RESEARCH,2019,47(16):8662-8674.
APA	Zhou, Xiao-Long,Chen, Yun,Zeng, Qi-Yu,Ruan, Zhi-Rong,Fang, Pengfei,&Wang, En-Duo.(2019).Newly acquired N-terminal extension targets threonyl-tRNA synthetase-like protein into the multiple tRNA synthetase complex.NUCLEIC ACIDS RESEARCH,47(16),8662-8674.
MLA	Zhou, Xiao-Long,et al."Newly acquired N-terminal extension targets threonyl-tRNA synthetase-like protein into the multiple tRNA synthetase complex".NUCLEIC ACIDS RESEARCH 47.16(2019):8662-8674.