Coexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode

	Coexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode
	Fang, ZP; Wang, M; Ruan, ZR; Tan, M; Liu, RJ; Zhou, M; Zhou, XL; Wang, ED
刊名	NUCLEIC ACIDS RESEARCH
	2014
卷号	42 期号:8 页码:5109-5124
通讯作者	Zhou, XL (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Ctr RNA Res,State Key Lab Mol Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,xlzhou@sibcb.ac.cn ; edwang@sibcb.ac.cn
英文摘要	Leucyl-tRNA (transfer RNA) synthetase (LeuRS) is a multi-domain enzyme, which is divided into bacterial and archaeal/eukaryotic types. In general, one specific LeuRS, the domains of which are of the same type, exists in a single cell compartment. However, some species, such as the haloalkaliphile Natrialba magadii, encode two cytoplasmic LeuRSs, NmLeuRS1 and NmLeuRS2, which are the first examples of naturally occurring chimeric enzymes with different domains of bacterial and archaeal types. Furthermore, N. magadii encodes typical archaeal tRNA(Leu)s. The tRNA recognition mode, aminoacylation and translational quality control activities of these two LeuRSs are interesting questions to be addressed. Herein, active NmLeuRS1 and NmLeuRS2 were successfully purified after gene expression in Escherichia coli. Under the optimized aminoacylation conditions, we discovered that they distinguished cognate NmtRNA(Leu) in the archaeal mode, whereas the N-terminal region was of the bacterial type. However, NmLeuRS1 exhibited much higher aminoacylation and editing activity than NmLeuRS2, suggesting that NmLeuRS1 is more likely to generate Leu-tRNA(Leu) for protein biosynthesis. Moreover, using NmLeuRS1 as a model, we demonstrated misactivation of several non-cognate amino acids, and accuracy of protein synthesis was maintained mainly via post-transfer editing. This comprehensive study of the NmLeuRS/tRNA(Leu) system provides a detailed understanding of the coevolution of aminoacyl-tRNA synthetases and tRNA.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	AMINOACYL-TRANSFER-RNA ; PROOFREADING FUNCTIONAL CYCLE ; GENETIC-CODE AMBIGUITY ; C-TERMINAL DOMAIN ; PROTEIN-BIOSYNTHESIS ; CRYSTAL-STRUCTURE ; AQUIFEX-AEOLICUS ; QUALITY-CONTROL ; CP1 DOMAIN ; 2 FORMS
收录类别	SCI
语种	英语
WOS记录号	WOS:000336092300039
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/216]
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	Fang, ZP,Wang, M,Ruan, ZR,et al. Coexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode[J]. NUCLEIC ACIDS RESEARCH,2014,42(8):5109-5124.
APA	Fang, ZP.,Wang, M.,Ruan, ZR.,Tan, M.,Liu, RJ.,...&Wang, ED.(2014).Coexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode.NUCLEIC ACIDS RESEARCH,42(8),5109-5124.
MLA	Fang, ZP,et al."Coexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode".NUCLEIC ACIDS RESEARCH 42.8(2014):5109-5124.