Two non-redundant fragments in the N-terminal peptide of human cytosolic methionyl-tRNA synthetase were indispensable for the multi-synthetase complex incorporation and enzyme activity
文献类型：期刊论文
| 作者 | He, R; Zu, LD; Yao, P; Chen, X; Wang, ED |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2009 |
| 卷号 | 1794期号:2页码:347-354 |
| 关键词 | Methionyl-tRNA synthetase Multi-synthetase complex Human cytoplasm Incorporation Activity |
| 通讯作者 | Wang, ED (reprint author), Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol,State Key Lab Mol Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,edwang@sibs.ac.cn |
| 英文摘要 | In human cytoplasm, nine aminoacyl-tRNA synthetases (aaRSs) and three protein factors form a multi-synthetase complex (MSC). Human cytosolic methionyl-tRNA synthetase (hcMetRS) is a component of the MSC. Sequence alignment revealed that hcMetRS has an N-terminal extension of 267 amino acid residues. This extension can be divided into three sub-domains: GST-like, GN, and GC sub-domains. The effect of each subdomain in the N-terminal extension of hcMetRS on enzymatic activity and incorporation into the MSC was studied. The results of cellular assay showed that the GST-like sub-domain was responsible for the incorporation of hcMetRS into the MSC. The entire N-terminal extension of hcMetRS is indispensable for the enzymatic activity. Deletion mutagenesis revealed that a seven-amino acid motif within the sub-domain GC was important for the activity of amino acid activation. A conserved proline residue within the seven-amino acid motif was crucial, while the other six residues were moderately important for the amino acid activation activity. Thus, the last 15 residues of previously defined N-terminal extension of hcMetRS was a part of the catalytic domain; whereas the first 252 residues of hcMetRS constitute the N-terminal extended domain of hcMetRS. The formerly defined N-terminal extension of hcMetRS possesses two functions of two different domains. (C) 2008 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | BINDING DOMAIN ; PROTEIN ; PURIFICATION ; TRANSLATION ; DISSECTION ; COFACTOR ; SUBUNIT ; SHEEP |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000262952600023 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1148]  |
| 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 | He, R,Zu, LD,Yao, P,et al. Two non-redundant fragments in the N-terminal peptide of human cytosolic methionyl-tRNA synthetase were indispensable for the multi-synthetase complex incorporation and enzyme activity[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2009,1794(2):347-354. |
| APA | He, R,Zu, LD,Yao, P,Chen, X,&Wang, ED.(2009).Two non-redundant fragments in the N-terminal peptide of human cytosolic methionyl-tRNA synthetase were indispensable for the multi-synthetase complex incorporation and enzyme activity.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1794(2),347-354. |
| MLA | He, R,et al."Two non-redundant fragments in the N-terminal peptide of human cytosolic methionyl-tRNA synthetase were indispensable for the multi-synthetase complex incorporation and enzyme activity".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1794.2(2009):347-354. |
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。