C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNA(Ser) and tRNA(Leu)

doi:10.1074/jbc.M115.699777

	C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNA(Ser) and tRNA(Leu)
	Ji, Quan-Quan 1; Fang, Zhi-Peng 1; Ye, Qing 1; Ruan, Zhi-Rong 1; Zhou, Xiao-Long 1; Wang, En-Duo1,2
	2016-02-12
发表期刊	JOURNAL OF BIOLOGICAL CHEMISTRY (IF:4.0[JCR-2023],4.4[5-Year])
ISSN	0021-9258
卷号	291 期号:7 页码:3613-3625
发表状态	已发表
DOI	10.1074/jbc.M115.699777
摘要	Leucyl-tRNA synthetase (LeuRS) is a multidomain enzyme that catalyzes Leu-tRNA(Leu) formation and is classified into bacterial and archaeal/eukaryotic types with significant diversity in the C-terminal domain (CTD). CTDs of both bacterial and archaeal LeuRSs have been reported to recognize tRNA(Leu) through different modes of interaction. In the human pathogen Candida albicans, the cytoplasmic LeuRS (CaLeuRS) is distinguished by its capacity to recognize a uniquely evolved chimeric tRNA(Ser) (CatRNA(Ser)(CAG)) in addition to its cognate CatRNA(Leu), leading to CUG codon reassignment. Our previous study showed that eukaryotic but not archaeal LeuRSs recognize this peculiar tRNA(Ser), suggesting the significance of their highly divergent CTDs in tRNA(Ser) recognition. The results of this study provided the first evidence of the indispensable function of the CTD of eukaryotic LeuRS in recognizing non-cognate CatRNA(Ser) and cognate CatRNA(Leu). Three lysine residues were identified as involved in mediating enzyme-tRNA interaction in the leucylation process: mutation of all three sites totally ablated the leucylation activity. The importance of the three lysine residues was further verified by gel mobility shift assays and complementation of a yeast leuS gene knock-out strain.
关键词	aminoacyl-tRNA synthetase C-terminal domain (carboxyl tail domain CTD) Candida albicans enzyme mechanism transfer RNA (tRNA) recognition tRNALeu tRNASer
收录类别	SCI ; EI
语种	英语
资助项目	Committee of Science and Technology in Shanghai[12JC1409700] ; Committee of Science and Technology in Shanghai[15ZR1446500]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000370854500039
出版者	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
EI入藏号	20161802318330
EI主题词	Amino acids ; Candida ; Enzymes
EI分类号	Biology:461.9 ; Organic Compounds:804.1 ; Food Products:822.3
WOS关键词	SERYL-TRANSFER-RNA ; ESCHERICHIA-COLI ; CRYSTAL-STRUCTURE ; QUALITY-CONTROL ; CUG CODON ; AMINOACYLATION ; BINDING ; ANTICODON ; IDENTITY ; COMPLEX
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/1923
专题	生命科学与技术学院_特聘教授组_王恩多组
通讯作者	Zhou, Xiao-Long; Wang, En-Duo
作者单位	1.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China 2.ShanghaiTech Univ, Sch Life Sci & Technol, 319 Yue Yang Rd, 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	Ji, Quan-Quan,Fang, Zhi-Peng,Ye, Qing,et al. C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNA(Ser) and tRNA(Leu)[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2016,291(7):3613-3625.
APA	Ji, Quan-Quan,Fang, Zhi-Peng,Ye, Qing,Ruan, Zhi-Rong,Zhou, Xiao-Long,&Wang, En-Duo.(2016).C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNA(Ser) and tRNA(Leu).JOURNAL OF BIOLOGICAL CHEMISTRY,291(7),3613-3625.
MLA	Ji, Quan-Quan,et al."C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNA(Ser) and tRNA(Leu)".JOURNAL OF BIOLOGICAL CHEMISTRY 291.7(2016):3613-3625.