Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module
文献类型：期刊论文
| 作者 | Yan, W; Ye, Q; Tan, M; Chen, X; Eriani, G; Wang, ED |
| 刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
 |
| 出版日期 | 2015 |
| 卷号 | 290期号:19页码:12256-12267 |
| 关键词 | aminoacyl tRNA Synthetase enzyme evolution protein synthesis transfer RNA (tRNA) aminoacylation editing stem contact fold |
| 通讯作者 | Wang, ED (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,edwang@sibcb.ac.cn |
| 英文摘要 | Background: A structural module following the KMSKS catalytic loop is conserved in most class I synthetases. Results: This module contributes to aminoacylation and editing of leucyl-tRNA synthetases (LeuRS). Conclusion: This module affects the activities of LeuRS in both a structure- and sequence-dependent manner. Significance: This work further extends the function of stem-contact fold in LeuRS. A conserved structural module following the KMSKS catalytic loop exhibits --- topology in class Ia and Ib aminoacyl-tRNA synthetases. However, the function of this domain has received little attention. Here, we describe the effect this module has on the aminoacylation and editing capacities of leucyl-tRNA synthetases (LeuRSs) by characterizing the key residues from various species. Mutation of highly conserved basic residues on the third -helix of this domain impairs the affinity of LeuRS for the anticodon stem of tRNA(Leu), which decreases both aminoacylation and editing activities. Two glycine residues on this -helix contribute to flexibility, leucine activation, and editing of LeuRS from Escherichia coli (EcLeuRS). Acidic residues on the -strand enhance the editing activity of EcLeuRS and sense the size of the tRNA(Leu) D-loop. Incorporation of these residues stimulates the tRNA-dependent editing activity of the chimeric minimalist enzyme Mycoplasma mobile LeuRS fused to the connective polypeptide 1 editing domain and leucine-specific domain from EcLeuRS. Together, these results reveal the stem contact-fold to be a functional as well as a structural linker between the catalytic site and the tRNA binding domain. Sequence comparison of the EcLeuRS stem contact-fold domain with editing-deficient enzymes suggests that key residues of this module have evolved an adaptive strategy to follow the editing functions of LeuRS. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | PROOFREADING FUNCTIONAL CYCLE ; ESCHERICHIA-COLI TRNA(LEU) ; ANGSTROM CRYSTAL-STRUCTURE ; QUALITY-CONTROL ; BINDING DOMAIN ; GENETIC-CODE ; RECOGNITION ; DYNAMICS ; REVEALS ; COMPLEX |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000354388600036 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/98]  |
| 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 | Yan, W,Ye, Q,Tan, M,et al. Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2015,290(19):12256-12267. |
| APA | Yan, W,Ye, Q,Tan, M,Chen, X,Eriani, G,&Wang, ED.(2015).Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module.JOURNAL OF BIOLOGICAL CHEMISTRY,290(19),12256-12267. |
| MLA | Yan, W,et al."Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module".JOURNAL OF BIOLOGICAL CHEMISTRY 290.19(2015):12256-12267. |
入库方式： OAI收割
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。