Literature DB >> 3902504

Interaction of methionine-specific tRNAs from Escherichia coli with immobilized elongation factor Tu.

W Fischer, T Doi, M Ikehara, E Ohtsuka, M Sprinzl.   

Abstract

The interaction of three different Met-tRNAsMet from E. coli with bacterial elongation factor (EF) Tu X GTP was investigated by affinity chromatography. Met-tRNAfMet which lacks the base pair at the end of the acceptor stem binds only weakly to EF-Tu X GTP, while Met-tRNAmMet has a high affinity for the elongation factor. A modified Met-tRNAfMet which has a C1-G72 base pair binds much more strongly to immobilized EF-Tu X GTP than the native aminoacyl(aa)-tRNA with non-base-paired C1A72 at this position, demonstrating that the base pair including the first nucleotide in the tRNA is one of the essential structural requirements for the aa-tRNA X EF-Tu X GTP ternary complex formation.

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Year:  1985        PMID： 3902504     DOI： 10.1016/0014-5793(85)80062-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  10 in total

1.  The 51-63 base pair of tRNA confers specificity for binding by EF-Tu.

Authors:  Lee E Sanderson; Olke C Uhlenbeck
Journal:  RNA       Date:  2007-04-20       Impact factor: 4.942

2.  The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.

Authors:  W H McClain; J Schneider; S Bhattacharya; K Gabriel
Journal:  Proc Natl Acad Sci U S A       Date:  1998-01-20       Impact factor: 11.205

3.  Ser-tRNAs from bovine mitochondrion form ternary complexes with bacterial elongation factor Tu and GTP.

Authors:  E Gebhardt-Singh; M Sprinzl
Journal:  Nucleic Acids Res       Date:  1986-09-25       Impact factor: 16.971

4.  The role of modified purine 64 in initiator/elongator discrimination of tRNA(iMet) from yeast and wheat germ.

Authors:  S Kiesewetter; G Ott; M Sprinzl
Journal:  Nucleic Acids Res       Date:  1990-08-25       Impact factor: 16.971

5.  Mutants of Escherichia coli formylmethionine tRNA: a single base change enables initiator tRNA to act as an elongator in vitro.

Authors:  B L Seong; U L RajBhandary
Journal:  Proc Natl Acad Sci U S A       Date:  1987-12       Impact factor: 11.205

6.  The Escherichia coli argU10(Ts) phenotype is caused by a reduction in the cellular level of the argU tRNA for the rare codons AGA and AGG.

Authors:  Kensaku Sakamoto; Satoshi Ishimaru; Takatsugu Kobayashi; James R Walker; Shigeyuki Yokoyama
Journal:  J Bacteriol       Date:  2004-09       Impact factor: 3.490

7.  Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis.

Authors:  Jared M Schrader; Stephen J Chapman; Olke C Uhlenbeck
Journal:  J Mol Biol       Date:  2009-03-13       Impact factor: 5.469

8.  Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA transformylase.

Authors:  C P Lee; M R Dyson; N Mandal; U Varshney; B Bahramian; U L RajBhandary
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-01       Impact factor: 11.205

9.  Crosslinking of elongation factor Tu to tRNA(Phe) by trans-diamminedichloroplatinum (II). Characterization of two crosslinking sites in the tRNA.

Authors:  F P Wikman; P Romby; M H Metz; J Reinbolt; B F Clark; J P Ebel; C Ehresmann; B Ehresmann
Journal:  Nucleic Acids Res       Date:  1987-07-24       Impact factor: 16.971

10.  Is the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria?

Authors:  Jared M Schrader; Olke C Uhlenbeck
Journal:  Nucleic Acids Res       Date:  2011-09-05       Impact factor: 16.971
  10 in total

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