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| A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities | |
| 2018-04-20 | |
| Source Publication | NUCLEIC ACIDS RESEARCH
 |
| ISSN | 0305-1048 |
| Volume | 46Issue:7Pages:3643-3656 |
| Status | 已发表 |
| DOI | 10.1093/nar/gky211 |
| Abstract | 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. |
| Indexed By | SCI ; SCIE |
| Language | 英语 |
| Funding Project | China Postdoctoral Science Foundation[2014T70438] |
| WOS Research Area | Biochemistry & Molecular Biology |
| WOS Subject | Biochemistry & Molecular Biology |
| WOS ID | WOS:000431137900034 |
| Publisher | OXFORD UNIV PRESS |
| WOS Keyword | TRANSLATIONAL QUALITY-CONTROL ; ACTIVE-SITE ; AMINO-ACIDS ; DOMAIN ; TRNA(LEU) ; NUCLEAR ; DISCRIMINATION ; BIOSYNTHESIS ; MECHANISM ; FIDELITY |
| Original Document Type | Article |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/20855 |
| 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_博士生 |
| Corresponding Author | Zhou, Xiao-Long; Wang, En-Duo |
| Affiliation | 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 |
| Corresponding Author Affilication | School of Life Science and Technology |
| Recommended Citation 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. |
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