Peripheral insertion modulates the editing activity of the isolated CP1 domain of leucyl-tRNA synthetase
文献类型：期刊论文
| 作者 | Liu, RJ; Tan, M; Du, DH; Xu, BS; Eriani, G; Wang, ED |
| 刊名 | BIOCHEMICAL JOURNAL
 |
| 出版日期 | 2011 |
| 卷号 | 440期号:1页码:217-227 |
| 关键词 | aminoacyl-tRNA synthetase Aquifex aeolicus connective peptide 1 (CP1) Giardia lamblia post-transfer editing tRNA |
| 通讯作者 | Wang, ED (reprint author), Chinese Acad Sci, State Key Lab Mol Biol, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,edwang@sibs.ac.cn |
| 英文摘要 | A large insertion domain called CP1 (connective peptide I) present in class Ia aminoacyl-tRNA synthetases is responsible for post-transfer editing. LeuRS (leucyl-tRNA synthetase) from Aquifex aeolicus and Giardia lamblia possess unique 20 and 59 amino acid insertions respectively within the CP1 that are crucial for editing activity. Crystal structures of AaLeuRS-CP1 [2.4 angstrom (1 angstrom = 0.1 nm)], G/LeuRS-CP1 (2.6 angstrom) and the insertion deletion mutant AaLeuRS-CP1 Delta 20 (2.5 angstrom) were solved to understand the role of these insertions in editing. Both insertions are folded as peripheral motifs located on the opposite side of the proteins from the active-site entrance in the CP1 domain. Docking modelling and site-directed mutagenesis showed that the insertions do not interact with the substrates. Results of molecular dynamics simulations show that the intact CP1 is more dynamic than its mutant devoid of the insertion motif. Taken together, the data show that a peripheral insertion without a substrate-binding site or major structural role in the active site may modulate catalytic function of a protein, probably from protein dynamics regulation in two respective LeuRS CP1s. Further results from proline and glycine mutational analyses intended to reduce or increase protein flexibility are consistent with this hypothesis. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | TRANSFER RIBONUCLEIC-ACID ; AMINO-ACID ; CRYSTAL-STRUCTURE ; STRUCTURAL BASIS ; PROTEIN ; DISCRIMINATION ; MECHANISM ; COMPLEX ; SPECIFICITY ; ISOLEUCINE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000298222200006 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/908]  |
| 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 | Liu, RJ,Tan, M,Du, DH,et al. Peripheral insertion modulates the editing activity of the isolated CP1 domain of leucyl-tRNA synthetase[J]. BIOCHEMICAL JOURNAL,2011,440(1):217-227. |
| APA | Liu, RJ,Tan, M,Du, DH,Xu, BS,Eriani, G,&Wang, ED.(2011).Peripheral insertion modulates the editing activity of the isolated CP1 domain of leucyl-tRNA synthetase.BIOCHEMICAL JOURNAL,440(1),217-227. |
| MLA | Liu, RJ,et al."Peripheral insertion modulates the editing activity of the isolated CP1 domain of leucyl-tRNA synthetase".BIOCHEMICAL JOURNAL 440.1(2011):217-227. |
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