Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution
文献类型：期刊论文
| 作者 | Zhao, MW; Zhu, B; Hao, R; Xu, MG; Eriani, G; Wang, ED |
| 刊名 | EMBO JOURNAL
 |
| 出版日期 | 2005 |
| 卷号 | 24期号:7页码:1430-1439 |
| 关键词 | Aquifex aeolicus CP1 domain editing leucyl-tRNA synthetase tRNA |
| 通讯作者 | Wang, ED (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol,Grad Sch, 320 Yeu Yang Rd, Shanghai 200031, Peoples R China.,edwang@sibs.ac.cn |
| 英文摘要 | The editing reactions catalyzed by aminoacyl-tRNA synthetases are critical for the faithful protein synthesis by correcting misactivated amino acids and misamino-acylated tRNAs. We report that the isolated editing domain of leucyl-tRNA synthetase from the deep-rooted bacterium Aquifex aeolicus (alpha beta-LeuRS) catalyzes the hydrolytic editing of both mischarged tRNA(Leu) and minihelix(Leu). Within the domain, we have identified a crucial 20-amino-acid peptide that confers editing capacity when transplanted into the inactive Escherichia coli LeuRS editing domain. Likewise, fusion of the beta-subunit of alpha beta-LeuRS to the E. coli editing domain activates its editing function. These results suggest that alpha beta-LeuRS still carries the basic features from a primitive synthetase molecule. It has a remarkable capacity to transfer autonomous active modules, which is consistent with the idea that modern synthetases arose after exchange of small idiosyncratic domains. It also has a unique alpha beta-heterodimeric structure with separated catalytic and tRNA-binding sites. Such an organization supports the tRNA/synthetase coevolution theory that predicts sequential addition of tRNA and synthetase domains. |
| 学科主题 | Biochemistry & Molecular Biology; Cell Biology |
| 类目[WOS] | Biochemistry & Molecular Biology ; Cell Biology |
| 关键词[WOS] | RIBONUCLEIC-ACID SYNTHETASE ; ESCHERICHIA-COLI ; CELL VIABILITY ; GENETIC-CODE ; PROTEIN-SYNTHESIS ; CRYSTAL-STRUCTURE ; INSERTION DOMAIN ; CP1 DOMAIN ; L-VALINE ; AMINOACYLATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000228327100013 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1939]  |
| 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 | Zhao, MW,Zhu, B,Hao, R,et al. Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution[J]. EMBO JOURNAL,2005,24(7):1430-1439. |
| APA | Zhao, MW,Zhu, B,Hao, R,Xu, MG,Eriani, G,&Wang, ED.(2005).Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution.EMBO JOURNAL,24(7),1430-1439. |
| MLA | Zhao, MW,et al."Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution".EMBO JOURNAL 24.7(2005):1430-1439. |
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