The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation
文献类型：期刊论文
| 作者 | Tan, M; Wang, M; Zhou, XL; Yan, W; Eriani, G; Wang, ED |
| 刊名 | NUCLEIC ACIDS RESEARCH
 |
| 出版日期 | 2013 |
| 卷号 | 41期号:10页码:5513-5523 |
| 通讯作者 | Wang, ED (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, State Key Lab Mol Biol, Inst Biochem & Cell Biol,Ctr RNA Res, Shanghai 200031, Peoples R China.,edwang@sibs.ac.cn |
| 英文摘要 | Faithful translation of the genetic code depends on accurate coupling of amino acids with cognate transfer RNAs (tRNAs) catalyzed by aminoacyl-tRNA synthetases. The fidelity of leucyl-tRNA synthetase (LeuRS) depends mainly on proofreading at the pre- and post-transfer levels. During the catalytic cycle, the tRNA CCA-tail shuttles between the synthetic and editing domains to accomplish the aminoacylation and editing reactions. Previously, we showed that the Y330D mutation of Escherichia coli LeuRS, which blocks the entry of the tRNA CCA-tail into the connective polypeptide 1domain, abolishes both tRNA-dependent pre- and post-transfer editing. In this study, we identified the counterpart substitutions, which constrain the tRNA acceptor stem binding within the synthetic active site. These mutations negatively impact the tRNA charging activity while retaining the capacity to activate the amino acid. Interestingly, the mutated LeuRSs exhibit increased global editing activity in the presence of a non-cognate amino acid. We used a reaction mimicking post-transfer editing to show that these mutations decrease post-transfer editing owing to reduced tRNA aminoacylation activity. This implied that the increased editing activity originates from tRNA-dependent pre-transfer editing. These results, together with our previous work, provide a comprehensive assessment of how intra-molecular translocation of the tRNA CCA-tail balances the aminoacylation and editing activities of LeuRS. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | ESCHERICHIA-COLI ; PRE-TRANSFER ; SYNTHETASE STRUCTURE ; CRYSTAL-STRUCTURE ; AMINO-ACIDS ; CP1 DOMAIN ; PATHWAYS ; TRNA(LEU) ; COMPLEX ; DISCRIMINATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000319806600036 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/439]  |
| 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 | Tan, M,Wang, M,Zhou, XL,et al. The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation[J]. NUCLEIC ACIDS RESEARCH,2013,41(10):5513-5523. |
| APA | Tan, M,Wang, M,Zhou, XL,Yan, W,Eriani, G,&Wang, ED.(2013).The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation.NUCLEIC ACIDS RESEARCH,41(10),5513-5523. |
| MLA | Tan, M,et al."The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation".NUCLEIC ACIDS RESEARCH 41.10(2013):5513-5523. |
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