Literature DB >> 7688564

In vitro analysis of translational rate and accuracy with an unmodified tRNA.

K M Harrington1, I A Nazarenko, D B Dix, R C Thompson, O C Uhlenbeck.   

Abstract

Escherichia coli tRNA(Phe) transcript lacking all the modified nucleosides was investigated in an in vitro translation system. To estimate the affinity of tRNA toward EF-Tu, Kd and K-1 were measured by the nuclease protection assay, and it was shown that the absence of modifications decreases ternary complex stability less than 2-fold. The activity of unmodified Phe-tRNA(Phe) on E. coli ribosomes was compared to modified Phe-tRNA(Phe) using the framework of the kinetic proofreading mechanism (Thompson & Dix, 1982) with both cognate and noncognate codons. Values of the individual rate constants in the elongation process showed that the modifications increased the accuracy of translation by (1) decreasing the rate of dipeptide synthesis and (2) increasing the rate of rejection with noncognate codons.

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Year:  1993        PMID: 7688564     DOI: 10.1021/bi00081a003

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  33 in total

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Authors:  Lauren Ancel Meyers; Jennifer F Lee; Matthew Cowperthwaite; Andrew D Ellington
Journal:  J Mol Evol       Date:  2004-06       Impact factor: 2.395

2.  Specificity of translation for N-alkyl amino acids.

Authors:  Baolin Zhang; Zhongping Tan; Lucas Gartenmann Dickson; Madhavi N L Nalam; Virginia W Cornish; Anthony C Forster
Journal:  J Am Chem Soc       Date:  2007-08-25       Impact factor: 15.419

3.  Slow peptide bond formation by proline and other N-alkylamino acids in translation.

Authors:  Michael Y Pavlov; Richard E Watts; Zhongping Tan; Virginia W Cornish; Måns Ehrenberg; Anthony C Forster
Journal:  Proc Natl Acad Sci U S A       Date:  2008-12-22       Impact factor: 11.205

4.  Perturbation of the tRNA tertiary core differentially affects specific steps of the elongation cycle.

Authors:  Dongli Pan; Chun-Mei Zhang; Stanislav Kirillov; Ya-Ming Hou; Barry S Cooperman
Journal:  J Biol Chem       Date:  2008-04-30       Impact factor: 5.157

5.  Codon-reading specificity of an unmodified form of Escherichia coli tRNA1Ser in cell-free protein synthesis.

Authors:  K Takai; H Takaku; S Yokoyama
Journal:  Nucleic Acids Res       Date:  1996-08-01       Impact factor: 16.971

6.  Highly conserved modified nucleosides influence Mg2+-dependent tRNA folding.

Authors:  Kelly N Nobles; Connie S Yarian; Guihua Liu; Richard H Guenther; Paul F Agris
Journal:  Nucleic Acids Res       Date:  2002-11-01       Impact factor: 16.971

7.  Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions.

Authors:  Andrey L Konevega; Natalia G Soboleva; Valentin I Makhno; Yuri P Semenkov; Wolfgang Wintermeyer; Marina V Rodnina; Vladimir I Katunin
Journal:  RNA       Date:  2004-01       Impact factor: 4.942

8.  Changeability of individual domains of an aminoacyl-tRNA in polymerization by the ribosome.

Authors:  Rong Gao; Anthony C Forster
Journal:  FEBS Lett       Date:  2010-01-04       Impact factor: 4.124

9.  The crystal structure of unmodified tRNAPhe from Escherichia coli.

Authors:  Robert T Byrne; Andrey L Konevega; Marina V Rodnina; Alfred A Antson
Journal:  Nucleic Acids Res       Date:  2010-03-04       Impact factor: 16.971

10.  tRNA residues evolved to promote translational accuracy.

Authors:  Irina Shepotinovskaya; Olke C Uhlenbeck
Journal:  RNA       Date:  2013-02-25       Impact factor: 4.942

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