Literature DB >> 23982864

Transfer RNA: a dancer between charging and mis-charging for protein biosynthesis.

Xiaolong Zhou1, Enduo Wang.   

Abstract

Transfer RNA plays a fundamental role in the protein biosynthesis as an adaptor molecule by functioning as a biological link between the genetic nucleotide sequence in the mRNA and the amino acid sequence in the protein. To perform its role in protein biosynthesis, it has to be accurately recognized by aminoacyl-tRNA synthetases (aaRSs) to generate aminoacyl-tRNAs (aa-tRNAs). The correct pairing between an amino acid with its cognate tRNA is crucial for translational quality control. Production and utilization of mis-charged tRNAs are usually detrimental for all the species, resulting in cellular dysfunctions. Correct aa-tRNAs formation is collectively controlled by aaRSs with distinct mechanisms and/or other trans-factors. However, in very limited instances, mis-charged tRNAs are intermediate for specific pathways or essential components for the translational machinery. Here, from the point of accuracy in tRNA charging, we review our understanding about the mechanism ensuring correct aa-tRNA generation. In addition, some unique mis-charged tRNA species necessary for the organism are also briefly described.

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Year:  2013        PMID: 23982864     DOI: 10.1007/s11427-013-4542-9

Source DB:  PubMed          Journal:  Sci China Life Sci        ISSN: 1674-7305            Impact factor:   6.038


  17 in total

1.  C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNASer and tRNALeu.

Authors:  Quan-Quan Ji; Zhi-Peng Fang; Qing Ye; Zhi-Rong Ruan; Xiao-Long Zhou; En-Duo Wang
Journal:  J Biol Chem       Date:  2015-12-16       Impact factor: 5.157

2.  Degenerate connective polypeptide 1 (CP1) domain from human mitochondrial leucyl-tRNA synthetase.

Authors:  Qing Ye; Meng Wang; Zhi-Peng Fang; Zhi-Rong Ruan; Quan-Quan Ji; Xiao-Long Zhou; En-Duo Wang
Journal:  J Biol Chem       Date:  2015-08-13       Impact factor: 5.157

3.  Identification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.

Authors:  Zhi-Rong Ruan; Zhi-Peng Fang; Qing Ye; Hui-Yan Lei; Gilbert Eriani; Xiao-Long Zhou; En-Duo Wang
Journal:  J Biol Chem       Date:  2014-11-21       Impact factor: 5.157

4.  Translational Quality Control by Bacterial Threonyl-tRNA Synthetases.

Authors:  Xiao-Long Zhou; Yun Chen; Zhi-Peng Fang; Zhi-Rong Ruan; Yong Wang; Ru-Juan Liu; Mei-Qin Xue; En-Duo Wang
Journal:  J Biol Chem       Date:  2016-08-19       Impact factor: 5.157

5.  Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.

Authors:  Yuchen Liu; Akiyoshi Nakamura; Yuto Nakazawa; Nozomi Asano; Kara A Ford; Michael J Hohn; Isao Tanaka; Min Yao; Dieter Söll
Journal:  Proc Natl Acad Sci U S A       Date:  2014-07-07       Impact factor: 11.205

6.  A Human Disease-causing Point Mutation in Mitochondrial Threonyl-tRNA Synthetase Induces Both Structural and Functional Defects.

Authors:  Yong Wang; Xiao-Long Zhou; Zhi-Rong Ruan; Ru-Juan Liu; Gilbert Eriani; En-Duo Wang
Journal:  J Biol Chem       Date:  2016-01-25       Impact factor: 5.157

7.  Distinct pathogenic mechanisms of various RARS1 mutations in Pelizaeus-Merzbacher-like disease.

Authors:  Guang Li; Gilbert Eriani; En-Duo Wang; Xiao-Long Zhou
Journal:  Sci China Life Sci       Date:  2021-01-28       Impact factor: 6.038

8.  Identification of determinants for tRNA substrate recognition by Escherichia coli C/U34 2'-O-methyltransferase.

Authors:  Mi Zhou; Tao Long; Zhi-Peng Fang; Xiao-Long Zhou; Ru-Juan Liu; En-Duo Wang
Journal:  RNA Biol       Date:  2015       Impact factor: 4.652

9.  Coexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode.

Authors:  Zhi-Peng Fang; Meng Wang; Zhi-Rong Ruan; Min Tan; Ru-Juan Liu; Mi Zhou; Xiao-Long Zhou; En-Duo Wang
Journal:  Nucleic Acids Res       Date:  2014-02-05       Impact factor: 16.971

10.  A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity.

Authors:  Qian Huang; Xiao-Long Zhou; Qin-Hua Hu; Hui-Yan Lei; Zhi-Peng Fang; Peng Yao; En-Duo Wang
Journal:  RNA       Date:  2014-07-22       Impact factor: 4.942

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