Aminoacylation and translational quality control strategy employed by leucyl-tRNA synthetase from a human pathogen with genetic code ambiguity

	Aminoacylation and translational quality control strategy employed by leucyl-tRNA synthetase from a human pathogen with genetic code ambiguity
	Zhou, XL; Fang, ZP; Ruan, ZR; Wang, M; Liu, RJ; Tan, M; Anella, FM; Wang, ED
刊名	NUCLEIC ACIDS RESEARCH
	2013
卷号	41 期号:21 页码:9825-9838
通讯作者	Wang, ED (reprint author), Chinese Acad Sci, Ctr RNA Res, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol,State Key Lab Mol Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,edwang@sibcb.ac.cn
英文摘要	Aminoacyl-tRNA synthetases should ensure high accuracy in tRNA aminoacylation. However, the absence of significant structural differences between amino acids always poses a direct challenge for some aminoacyl-tRNA synthetases, such as leucyl-tRNA synthetase (LeuRS), which require editing function to remove mis-activated amino acids. In the cytoplasm of the human pathogen Candida albicans, the CUG codon is translated as both Ser and Leu by a uniquely evolved CatRNA(Ser)(CAG). Its cytoplasmic LeuRS (CaLeuRS) is a crucial component for CUG codon ambiguity and harbors only one CUG codon at position 919. Comparison of the activity of CaLeuRS-Ser(919) and CaLeuRS-Leu(919) revealed yeast LeuRSs have a relaxed tRNA recognition capacity. We also studied the mis-activation and editing of non-cognate amino acids by CaLeuRS. Interestingly, we found that CaLeuRS is naturally deficient in tRNA-dependent pre-transfer editing for non-cognate norvaline while displaying a weak tRNA-dependent pre-transfer editing capacity for non-cognate alpha-amino butyric acid. We also demonstrated that post-transfer editing of CaLeuRS is not tRNA(Leu) species-specific. In addition, other eukaryotic but not archaeal or bacterial LeuRSs were found to recognize CatRNA(Ser)(CAG). Overall, we systematically studied the aminoacylation and editing properties of CaLeuRS and established a characteristic LeuRS model with naturally deficient tRNA-dependent pre-transfer editing, which increases LeuRS types with unique editing patterns.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	SPECIES-SPECIFIC AMINOACYLATION ; NONCOGNATE AMINO-ACIDS ; ESCHERICHIA-COLI ; CRYSTAL-STRUCTURE ; CANDIDA-ALBICANS ; CP1 DOMAIN ; TRNA(LEU) ; RECOGNITION ; NORVALINE ; IDENTITY
收录类别	SCI
语种	英语
WOS记录号	WOS:000327541800025
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/464]
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	Zhou, XL,Fang, ZP,Ruan, ZR,et al. Aminoacylation and translational quality control strategy employed by leucyl-tRNA synthetase from a human pathogen with genetic code ambiguity[J]. NUCLEIC ACIDS RESEARCH,2013,41(21):9825-9838.
APA	Zhou, XL.,Fang, ZP.,Ruan, ZR.,Wang, M.,Liu, RJ.,...&Wang, ED.(2013).Aminoacylation and translational quality control strategy employed by leucyl-tRNA synthetase from a human pathogen with genetic code ambiguity.NUCLEIC ACIDS RESEARCH,41(21),9825-9838.
MLA	Zhou, XL,et al."Aminoacylation and translational quality control strategy employed by leucyl-tRNA synthetase from a human pathogen with genetic code ambiguity".NUCLEIC ACIDS RESEARCH 41.21(2013):9825-9838.