Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote
文献类型：期刊论文
| 作者 | Zhou, XL; Ruan, ZR; Huang, Q; Tan, M; Wang, ED |
| 刊名 | NUCLEIC ACIDS RESEARCH
 |
| 出版日期 | 2013 |
| 卷号 | 41期号:1页码:302-314 |
| 通讯作者 | Wang, ED (reprint author), Chinese Acad Sci, State Key Lab Mol Biol, Inst Biochem & Cell Biol, Ctr RNA Res,Shanghai Inst Biol Sci, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,edwang@sibcb.ac.cn |
| 英文摘要 | Aminoacyl-tRNA synthetase (aaRS) catalyzes the first step of protein synthesis, producing aminoacyl-tRNAs as building blocks. Eukaryotic aaRS differs from its prokaryotic counterpart in terminal extension or insertion. Moreover, the editing function of aaRSs is an indispensable checkpoint excluding non-cognate amino acids at a given codon and ensuring overall translational fidelity. We found higher eukaryotes encode two cytoplasmic threonyl-tRNA synthetases (ThrRSs) with difference in N-terminus. The longer isoform is more closely related to the ThrRSs of higher eukaryotes than to those of lower eukaryotes. A yeast strain was generated to include deletion of the thrS gene encoding ThrRS. Combining in vitro biochemical and in vivo genetic data, ThrRSs from eukaryotic cytoplasm were systematically analyzed, and role of the eukaryotic cytoplasmic ThrRS-specific N-terminal extension was elucidated. Furthermore, the mechanisms of aminoacylation and editing activity mediated by Saccharomyces cerevisiae ThrRS (ScThrRS) were clarified. Interestingly, yeast cells were tolerant of variation at the editing active sites of ScThrRS without significant Thr-to-Ser conversion in the proteome even under significant environmental stress, implying checkpoints downstream of aminoacylation to provide a further quality control mechanism for the yeast translation system. This study has provided the first comprehensive elucidation of the translational fidelity control mechanism of eukaryotic ThrRS. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | TRANSFER-RNA-SYNTHETASE ; AMINOACYL-TRANSFER-RNA ; QUALITY-CONTROL ; EDITING MECHANISM ; ZINC ION ; 2 FORMS ; DOMAIN ; DISCRIMINATION ; IDENTITY ; ARCHAEA |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000312889900057 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/326]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Zhou, XL,Ruan, ZR,Huang, Q,et al. Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote[J]. NUCLEIC ACIDS RESEARCH,2013,41(1):302-314. |
| APA | Zhou, XL,Ruan, ZR,Huang, Q,Tan, M,&Wang, ED.(2013).Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote.NUCLEIC ACIDS RESEARCH,41(1),302-314. |
| MLA | Zhou, XL,et al."Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote".NUCLEIC ACIDS RESEARCH 41.1(2013):302-314. |
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