A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities

doi:10.1093/nar/gky211

	A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities
	Chen, Yun 1; Ruan, Zhi-Rong 1; Wang, Yong1,2 ; Huang, Qian 1; Xue, Mei-Qin 1; Zhou, Xiao-Long 1; Wang, En-Duo1,2
	2018-04-20
发表期刊	NUCLEIC ACIDS RESEARCH (IF:16.6[JCR-2023],16.1[5-Year])
ISSN	0305-1048
卷号	46 期号:7 页码:3643-3656
发表状态	已发表
DOI	10.1093/nar/gky211
摘要	TARS and TARS2 encode cytoplasmic and mitochondrial threonyl-tRNA synthetases (ThrRSs) in mammals, respectively. Interestingly, in higher eukaryotes, a third gene, TARSL2, encodes a ThrRS-like protein (ThrRS-L), which is highly homologous to cytoplasmic ThrRS but with a different N-terminal extension (N-extension). Whether ThrRS-L has canonical functions is unknown. In this work, we studied the organ expression pattern, cellular localization, canonical aminoacylation and editing activities of mouse ThrRS-L (mThrRS-L). Tarsl2 is ubiquitously but unevenly expressed in mouse tissues. Different from mouse cytoplasmic ThrRS (mThrRS), mThrRS-L is located in both the cytoplasm and nucleus; the nuclear distribution is mediated via a nuclear localization sequence at its C-terminus. Native mThrRS-L enriched from HEK293T cells was active in aminoacylation and editing. To investigate the in vitro catalytic properties of mThrRS-L accurately, we replaced the N-extension of mThrRS-L with that of mThrRS. The chimeric protein (mThrRS-L-NT) has amino acid activation, aminoacylation and editing activities. We compared the activities and cross-species tRNA recognition between mThrRS-L-NT and mThrRS. Despite having a similar aminoacylation activity, mThrRS-L-NT and mThrRS exhibit differences in tRNA recognition and editing capacity. Our results provided the first analysis of the aminoacylation and editing activities of ThrRS-L, and improved our understanding of Tarsl2.
收录类别	SCI ; SCIE
语种	英语
资助项目	China Postdoctoral Science Foundation[2014T70438]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000431137900034
出版者	OXFORD UNIV PRESS
WOS关键词	TRANSLATIONAL QUALITY-CONTROL ; ACTIVE-SITE ; AMINO-ACIDS ; DOMAIN ; TRNA(LEU) ; NUCLEAR ; DISCRIMINATION ; BIOSYNTHESIS ; MECHANISM ; FIDELITY
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/20855
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_博士生
通讯作者	Zhou, Xiao-Long; Wang, En-Duo
作者单位	1.Univ Chinese Acad Sci, CAS Ctr Excellence Mol Cell Sci, Shanghai Inst Biochem & Cell Biol, State Key Lab Mol Biol,Chinese Acad Sci, 320 Yue Yang Rd, Shanghai, Peoples R China 2.ShanghaiTech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai, 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	Chen, Yun,Ruan, Zhi-Rong,Wang, Yong,et al. A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities[J]. NUCLEIC ACIDS RESEARCH,2018,46(7):3643-3656.
APA	Chen, Yun.,Ruan, Zhi-Rong.,Wang, Yong.,Huang, Qian.,Xue, Mei-Qin.,...&Wang, En-Duo.(2018).A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities.NUCLEIC ACIDS RESEARCH,46(7),3643-3656.
MLA	Chen, Yun,et al."A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities".NUCLEIC ACIDS RESEARCH 46.7(2018):3643-3656.