中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Role of tRNA amino acid-accepting end in aminoacylation and its quality control

文献类型:期刊论文

作者Zhou, XL; Du, DH; Tan, M; Lei, HY; Ruan, LL; Eriani, G; Wang, ED
刊名NUCLEIC ACIDS RESEARCH
出版日期2011
卷号39期号:20页码:8857-8868
通讯作者Wang, ED (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China.,edwang@sibs.ac.cn
英文摘要Aminoacyl-tRNA synthetases (aaRSs) are remarkable enzymes that are in charge of the accurate recognition and ligation of amino acids and tRNA molecules. The greatest difficulty in accurate aminoacylation appears to be in discriminating between highly similar amino acids. To reduce mischarging of tRNAs by non-cognate amino acids, aaRSs have evolved an editing activity in a second active site to cleave the incorrect aminoacyl-tRNAs. Editing occurs after translocation of the aminoacyl-CCA(76) end to the editing site, switching between a hairpin and a helical conformation for aminoacylation and editing. Here, we studied the consequence of nucleotide changes in the CCA(76) accepting end of tRNA(Leu) during the aminoacylation and editing reactions. The analysis showed that the terminal A(76) is essential for both reactions, suggesting that critical interactions occur in the two catalytic sites. Substitutions of C(74) and C(75) selectively decreased aminoacylation keeping nearly unaffected editing. These mutations might favor the regular helical conformation required to reach the editing site. Mutating the editing domain residues that contribute to CCA(76) binding reduced the aminoacylation fidelity leading to cell-toxicity in the presence of non-cognate amino acids. Collectively, the data show how protein synthesis quality is controlled by the CCA(76) homogeneity of tRNAs.
学科主题Biochemistry & Molecular Biology
类目[WOS]Biochemistry & Molecular Biology
关键词[WOS]CCA-ADDING ENZYME ; LEUCYL-TRANSFER ; CRYSTAL-STRUCTURE ; AQUIFEX-AEOLICUS ; SYNTHETASE ; TRNA(LEU) ; RECOGNITION ; COMPLEX ; DOMAIN ; DISCRIMINATION
收录类别SCI
语种英语
WOS记录号WOS:000296343400024
版本出版稿
源URL[http://202.127.25.143/handle/331003/881]  
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,Du, DH,Tan, M,et al. Role of tRNA amino acid-accepting end in aminoacylation and its quality control[J]. NUCLEIC ACIDS RESEARCH,2011,39(20):8857-8868.
APA Zhou, XL.,Du, DH.,Tan, M.,Lei, HY.,Ruan, LL.,...&Wang, ED.(2011).Role of tRNA amino acid-accepting end in aminoacylation and its quality control.NUCLEIC ACIDS RESEARCH,39(20),8857-8868.
MLA Zhou, XL,et al."Role of tRNA amino acid-accepting end in aminoacylation and its quality control".NUCLEIC ACIDS RESEARCH 39.20(2011):8857-8868.

入库方式: OAI收割

来源:上海生物化学与细胞生物学研究所

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