A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity
文献类型：期刊论文
| 作者 | Huang, Q; Zhou, XL; Hu, QH; Lei, HY; Fang, ZP; Yao, P; Wang, ED |
| 刊名 | RNA-A PUBLICATION OF THE RNA SOCIETY
 |
| 出版日期 | 2014 |
| 卷号 | 20期号:9页码:1440-1450 |
| 关键词 | Homo sapiens cytoplasm leucyl-tRNA synthetase CP1 hairpin amino acid activation aminoacylation tRNA binding |
| 通讯作者 | Wang, ED (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Ctr RNA Res,State Key Lab Mol Biol, Shanghai 200031, Peoples R China.,edwang@sibcb.ac.cn |
| 英文摘要 | Leucyl-tRNA synthetases (LeuRSs) catalyze the linkage of leucine with tRNA(Leu). LeuRS contains a catalysis domain (aminoacylation) and a CP1 domain (editing). CP1 is inserted 35 A from the aminoacylation domain. Aminoacylation and editing require CP1 to swing to the coordinated conformation. The neck between the CP1 domain and the aminoacylation domain is defined as the CP1 hairpin. The location of the CP1 hairpin suggests a crucial role in the CP1 swing and domain domain interaction. Here, the CP1 hairpin of Homo sapiens cytoplasmic LeuRS (hcLeuRS) was deleted or substituted by those from other representative species. Lack of a CP1 hairpin led to complete loss of aminoacylation, amino acid activation, and tRNA binding; however, the mutants retained post-transfer editing. Only the CP1 hairpin from Saccharomyces cerevisiae LeuRS (ScLeuRS) could partly rescue the hcLeuRS functions. Further site-directed mutagenesis indicated that the flexibility of small residues and the charge of polar residues in the CP1 hairpin are crucial for the function of LeuRS. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | QUALITY-CONTROL ; PROTEIN-BIOSYNTHESIS ; CRYSTAL-STRUCTURE ; MISTRANSLATION ; COMMUNICATION ; COMPLEX ; SITE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000341067300010 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/227]  |
| 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 | Huang, Q,Zhou, XL,Hu, QH,et al. A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity[J]. RNA-A PUBLICATION OF THE RNA SOCIETY,2014,20(9):1440-1450. |
| APA | Huang, Q.,Zhou, XL.,Hu, QH.,Lei, HY.,Fang, ZP.,...&Wang, ED.(2014).A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity.RNA-A PUBLICATION OF THE RNA SOCIETY,20(9),1440-1450. |
| MLA | Huang, Q,et al."A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity".RNA-A PUBLICATION OF THE RNA SOCIETY 20.9(2014):1440-1450. |
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