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

	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
	He, R; Zu, LD; Yao, P; Chen, X; Wang, ED
刊名	BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
	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
内容类型	期刊论文
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.