A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity

	A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity
	Tan, M; Yan, W; Liu, RJ; Wang, M; Chen, X; Zhou, XL; Wang, ED
刊名	BIOCHEMICAL JOURNAL
	2012
卷号	443 期号:1 页码:477-484
关键词	aminoacylation CP1 (connective peptide 1) domain RNA editing evolution leucyl-tRNA synthetase
通讯作者	Wang, ED (reprint author), Chinese Acad Sci, State Key Lab Mol Biol, Ctr RNA Res, 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	aaRSs (aminoacyl-tRNA synthetases) establish the rules of the genetic code by catalysing the formation of aminoacyl-tRNA. The quality control for arninoacylation is achieved by editing activity, which is usually carried out by a discrete editing domain. For LeuRS (leucyl-tRNA synthetase), the CP1 (connective peptide 1) domain is the editing domain responsible for hydrolysing mischarged tRNA. The CP1 domain is universally present in LeuRSs, except MmLeuRS (Mycoplasma mobile LeuRS). The substitute of CP1 in MmLeuRS is a nonapeptide (MmLinker). In the present study, we show that the MmLinker, which is critical for the aminoacylation activity of MmLeuRS, could confer remarkable tRNA-charging activity on the inactive CP1-deleted LeuRS from Escherichia coli (EcLeuRS) and Aquifex aeolicus (AaLeuRS). Furthermore, CP1 from EcLeuRS could functionally compensate for the MmLinker and endow MmLeuRS with post-transfer editing capability. These investigations provide a mechanistic framework for the modular construction of aaRSs and their co-ordination to achieve catalytic efficiency and fidelity. These results also show that the pre-transfer editing function of LeuRS originates from its conserved synthetic domain and shed light on future study of the mechanism.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	GENETIC-CODE ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; AQUIFEX-AEOLICUS ; QUALITY-CONTROL ; MISTRANSLATION ; TRNA(LEU) ; COMPLEX ; RECOGNITION ; PATHWAYS
收录类别	SCI
语种	英语
WOS记录号	WOS:000303096600015
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/705]
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	Tan, M,Yan, W,Liu, RJ,et al. A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity[J]. BIOCHEMICAL JOURNAL,2012,443(1):477-484.
APA	Tan, M.,Yan, W.,Liu, RJ.,Wang, M.,Chen, X.,...&Wang, ED.(2012).A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity.BIOCHEMICAL JOURNAL,443(1),477-484.
MLA	Tan, M,et al."A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity".BIOCHEMICAL JOURNAL 443.1(2012):477-484.