A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity

doi:10.1261/rna.044404.114

	A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity
	Huang, Qian 1; Zhou, Xiao-Long 1; Hu, Qin-Hua 1; Lei, Hui-Yan 1; Fang, Zhi-Peng 1; Yao, Peng 1; Wang, En-Duo1,2
	2014-09
发表期刊	RNA (IF:4.2[JCR-2023],4.4[5-Year])
ISSN	1355-8382
卷号	20 期号:9 页码:1440-1450
发表状态	已发表
DOI	10.1261/rna.044404.114
摘要	Leucyl-tRNA synthetases (LeuRSs) catalyze the linkage of leucine with tRNA(Leu). LeuRS contains a catalysis domain (aminoacylation) and a CP1 domain (editing). CP1 is inserted 35 A from the aminoacylation domain. Aminoacylation and editing require CP1 to swing to the coordinated conformation. The neck between the CP1 domain and the aminoacylation domain is defined as the CP1 hairpin. The location of the CP1 hairpin suggests a crucial role in the CP1 swing and domain domain interaction. Here, the CP1 hairpin of Homo sapiens cytoplasmic LeuRS (hcLeuRS) was deleted or substituted by those from other representative species. Lack of a CP1 hairpin led to complete loss of aminoacylation, amino acid activation, and tRNA binding; however, the mutants retained post-transfer editing. Only the CP1 hairpin from Saccharomyces cerevisiae LeuRS (ScLeuRS) could partly rescue the hcLeuRS functions. Further site-directed mutagenesis indicated that the flexibility of small residues and the charge of polar residues in the CP1 hairpin are crucial for the function of LeuRS.
关键词	Homo sapiens cytoplasm leucyl-tRNA synthetase CP1 hairpin amino acid activation aminoacylation tRNA binding
收录类别	SCI
语种	英语
资助项目	China Postdoctoral Science Foundation[2013M541562] ; China Postdoctoral Science Foundation[2014T70438]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000341067300010
出版者	COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
WOS关键词	QUALITY-CONTROL ; PROTEIN-BIOSYNTHESIS ; CRYSTAL-STRUCTURE ; MISTRANSLATION ; COMMUNICATION ; COMPLEX ; SITE
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/2380
专题	生命科学与技术学院_特聘教授组_王恩多组
通讯作者	Wang, En-Duo
作者单位	1.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Ctr RNA Res,State Key Lab Mol Biol, Shanghai 200031, Peoples R China 2.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 200031, Peoples R China
通讯作者单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Huang, Qian,Zhou, Xiao-Long,Hu, Qin-Hua,et al. A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity[J]. RNA,2014,20(9):1440-1450.
APA	Huang, Qian.,Zhou, Xiao-Long.,Hu, Qin-Hua.,Lei, Hui-Yan.,Fang, Zhi-Peng.,...&Wang, En-Duo.(2014).A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity.RNA,20(9),1440-1450.
MLA	Huang, Qian,et al."A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity".RNA 20.9(2014):1440-1450.