Translational Quality Control by Bacterial Threonyl-tRNA Synthetases

doi:10.1074/jbc.M116.740472

	Translational Quality Control by Bacterial Threonyl-tRNA Synthetases
	Zhou, Xiao-Long 1; Chen, Yun 1; Fang, Zhi-Peng 1; Ruan, Zhi-Rong 1; Wang, Yong2 ; Liu, Ru-Juan 1; Xue, Mei-Qin 1; Wang, En-Duo1,2
	2016-09-30
发表期刊	JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN	0021-9258
卷号	291 期号:40 页码:21208-21221
发表状态	已发表
DOI	10.1074/jbc.M116.740472
摘要	Translational fidelity mediated by aminoacyl-tRNA synthetases ensures the generation of the correct aminoacyl-tRNAs, which is critical for most species. Threonyl-tRNA synthetase (ThrRS) contains multiple domains, including an N2 editing domain. Of the ThrRS domains, N1 is the last to be assigned a function. Here, we found that ThrRSs from Mycoplasma species exhibit differences in their domain composition and editing active sites compared with the canonical ThrRSs. The Mycoplasma mobile ThrRS, the first example of a ThrRS naturally lacking the N1 domain, displays efficient post-transfer editing activity. In contrast, the Mycoplasma capricolum ThrRS, which harbors an N1 domain and a degenerate N2 domain, is editing-defective. Only editing-capable ThrRSs were able to support the growth of a yeast thrS deletion strain (Sc Delta thrS), thus suggesting that Sc Delta thrS is an excellent tool for studying the in vivo editing of introduced bacterial ThrRSs. On the basis of the presence or absence of an N1 domain, we further revealed the crucial importance of the only absolutely conserved residue within the N1 domain in regulating editing by mediating an N1-N2 domain interaction in Escherichia coli ThrRS. Our results reveal the translational quality control of various ThrRSs and the role of the N1 domain in translational fidelity.
收录类别	SCI ; EI
语种	英语
资助项目	Shanghai Rising-Star Program Grant[16QA1404400]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000385406200034
出版者	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
EI入藏号	20164002872735
EI主题词	Amino acids ; Bacteria ; Enzyme inhibition ; Escherichia coli
EI分类号	Organic Compounds:804.1 ; Quality Assurance and Control:913.3
WOS关键词	GENETIC-CODE ; PROTEIN-BIOSYNTHESIS ; AMINOACYLATION ; DOMAIN ; MISTRANSLATION ; TRNA(LEU) ; COMPLEX ; YEAST ; DISCRIMINATION ; RECOGNITION
原始文献类型	Article
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1699
专题	生命科学与技术学院生命科学与技术学院_特聘教授组_王恩多组生命科学与技术学院_博士生
通讯作者	Wang, En-Duo
作者单位	1.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol,Ctr Excellence Mol Cell Sc, 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	Zhou, Xiao-Long,Chen, Yun,Fang, Zhi-Peng,et al. Translational Quality Control by Bacterial Threonyl-tRNA Synthetases[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2016,291(40):21208-21221.
APA	Zhou, Xiao-Long.,Chen, Yun.,Fang, Zhi-Peng.,Ruan, Zhi-Rong.,Wang, Yong.,...&Wang, En-Duo.(2016).Translational Quality Control by Bacterial Threonyl-tRNA Synthetases.JOURNAL OF BIOLOGICAL CHEMISTRY,291(40),21208-21221.
MLA	Zhou, Xiao-Long,et al."Translational Quality Control by Bacterial Threonyl-tRNA Synthetases".JOURNAL OF BIOLOGICAL CHEMISTRY 291.40(2016):21208-21221.