The mRNA of Human Cytoplasmic Arginyl-tRNA Synthetase Recruits Prokaryotic Ribosomes Independently

doi:10.1074/jbc.M114.562454

	The mRNA of Human Cytoplasmic Arginyl-tRNA Synthetase Recruits Prokaryotic Ribosomes Independently
	Yang, Fang 1; Ji, Quan-Quan 1; Ruan, Liang-Liang 1; Ye, Qing 1; Wang, En-Duo1,2
	2014-07-25
发表期刊	JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN	0021-9258
卷号	289 期号:30 页码:20953-20959
发表状态	已发表
DOI	10.1074/jbc.M114.562454
摘要	There are two isoforms of cytoplasmic arginyl-tRNA synthetase (hcArgRS) in human cells. The long form is a component of the multiple aminoacyl-tRNA synthetase complex, and the other is an N-terminal truncated form (Delta NhcArgRS), free in the cytoplasm. It has been shown that the two forms of ArgRS arise from alternative translational initiation in a single mRNA. The short form is produced from the initiation at a downstream, in-frame AUG start codon. Interestingly, our data suggest that the alternative translational initiation of hcArgRS mRNA also takes place in Escherichia coli transformants. When the gene encoding full-length hcArgRS was overexpressed in E. coli, two forms of hcArgRS were observed. The N-terminal sequencing experiment identified that the short form was identical to the Delta NhcArgRS in human cytoplasm. By constructing a bicistronic system, our data support that the mRNA encoding the N-terminal extension of hcArgRS has the capacity of independently recruiting E. coli ribosomes. Furthermore, two critical elements for recruiting prokaryotic ribosomes were identified, the "AGGA" core of the Shine-Dalgarno sequence and the "A-rich" sequence located just proximal to the alternative in-frame initiation site. Although the mechanisms of prokaryotic and eukaryotic translational initiation are distinct, they share some common features. The ability of the hcArgRS mRNA to recruit the prokaryotic ribosome may provide clues for shedding light on the mechanism of alternative translational initiation of hcArgRS mRNA in eukaryotic cells.
收录类别	SCI ; EI
语种	英语
资助项目	Natural Key Basic Research Foundation of China[2012CB911001]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000339396600048
出版者	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
EI入藏号	20143218044721
EI主题词	Amino acids ; Cells ; Cytology ; Escherichia coli ; Gene encoding
EI分类号	Bioengineering and Biology:461 ; Atomic and Molecular Physics:931.3
WOS关键词	AMINOACYL-TRANSFER RNA ; TRANSLATION INITIATION ; SECONDARY STRUCTURE ; 2 FORMS ; REINITIATION ; SEQUENCE ; EUKARYOTES ; COMPLEX ; DOMAIN ; SHINE
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/2387
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	Yang, Fang,Ji, Quan-Quan,Ruan, Liang-Liang,et al. The mRNA of Human Cytoplasmic Arginyl-tRNA Synthetase Recruits Prokaryotic Ribosomes Independently[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2014,289(30):20953-20959.
APA	Yang, Fang,Ji, Quan-Quan,Ruan, Liang-Liang,Ye, Qing,&Wang, En-Duo.(2014).The mRNA of Human Cytoplasmic Arginyl-tRNA Synthetase Recruits Prokaryotic Ribosomes Independently.JOURNAL OF BIOLOGICAL CHEMISTRY,289(30),20953-20959.
MLA	Yang, Fang,et al."The mRNA of Human Cytoplasmic Arginyl-tRNA Synthetase Recruits Prokaryotic Ribosomes Independently".JOURNAL OF BIOLOGICAL CHEMISTRY 289.30(2014):20953-20959.