Literature DB >> 1091915

Study of the role of the acceptor stem in the interactions between tRNAs and aminoacyl-tRNA synthetases.

J Bonnet, N Befort, C Bollack, F Fasiolo, J P Ebel.   

Abstract

Several studies have clearly demonstrated that the end of the acceptor stem was a very important area determining the aminoacylation properties of tRNAs. However the attempts to measure the contribution of this region to the binding of tRNAs to aminoacyl-tRNA synthetases have led to contradictory results. We report here the stepwise degradation of yeast tRNA-Phe and tRNA-Val from their 3' terminus, up to the seventh nucleotide : the affinity of each of the degraded-tRNA for their cognate aminoacyl-tRNA synthetase was compared to that of intact tRNA and it was found that these affinities are not significantly decreased when compared to those of the intact tRNAs.

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Year:  1975        PMID： 1091915      PMCID： PMC342827          DOI： 10.1093/nar/2.2.211

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN： 0305-1048            Impact factor:   16.971


  18 in total

1.  Loss of methionine acceptor activity resulting from a base change in the anticodon of Escherichia coli formylmethionine transfer ribonucleic acid.

Authors:  L H Schulman; J P Goddard
Journal:  J Biol Chem       Date:  1973-02-25       Impact factor: 5.157

2.  Is there a discriminator site in transfer RNA?

Authors:  D M Crothers; T Seno; G Söll
Journal:  Proc Natl Acad Sci U S A       Date:  1972-10       Impact factor: 11.205

Review 3.  Synthesis and functions of the -C-C-A terminus of transfer RNA.

Authors:  M P Deutscher
Journal:  Prog Nucleic Acid Res Mol Biol       Date:  1973

4.  Amino acid acceptor stem of E. coli suppressor tRNA tyr is a site of synthetase recognition.

Authors:  J E Celis; M L Hooper; J D Smith
Journal:  Nat New Biol       Date:  1973-08-29

5.  Factors determining the specificity of the tRNA aminoacylation reaction. Non-absolute specificity of tRNA-aminoacyl-tRNA synthetase recognition and particular importance of the maximal velocity.

Authors:  J P Ebel; R Giegé; J Bonnet; D Kern; N Befort; C Bollack; F Fasiolo; J Gangloff; G Dirheimer
Journal:  Biochimie       Date:  1973-05       Impact factor: 4.079

6.  Inactivation of valine acceptor ativity by a C-U missense change in the anticodon of yeast valine transfer ribonucleic acid.

Authors:  R W Chambers; S Aoyagi; Y Furukawa; H Zawadzka; O S Bhanot
Journal:  J Biol Chem       Date:  1973-08-10       Impact factor: 5.157

7.  Structure and function of transfer ribonucleic acid. IV. Complexes between valyl transfer ribonucleic acid synthetase and structurally modified transfer ribonucleic acid specific for valine.

Authors:  U Lagerkvist; L Rymo
Journal:  J Biol Chem       Date:  1970-01-25       Impact factor: 5.157

8.  Sequential degradation of nucleic acids. Degradation of Escherichia coli B phenylalanine transfer ribonucleic acid.

Authors:  M Uziel; J X Khym
Journal:  Biochemistry       Date:  1969-08       Impact factor: 3.162

9.  Columns for rapid chromatographic separation of small amounts of tracer-labeled transfer ribonucleic acids.

Authors:  A D Kelmers; D E Heatherly
Journal:  Anal Biochem       Date:  1971-12       Impact factor: 3.365

10.  Chemically modified phenylalanine transfer ribonucleic acid from yeast. Synthesis and properties of tRNA Phe-C-Cs-A and the effect of adenosine 5'-O-(1-thiotriphosphate) on the activation of phenylalanine.

Authors:  E Schlimme; F von der Haar; F Eckstein; F Cramer
Journal:  Eur J Biochem       Date:  1970-06
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  1 in total

1.  Conformational activation of the yeast phenylalanyl-tRNA synthetase catalytic site induced by tRNAPhe interaction: triggering of adenosine or CpCpA trinucleoside diphosphate aminoacylation upon binding of tRNAPhe lacking these residues.

Authors:  M Renaud; H Bacha; P Remy; J P Ebel
Journal:  Proc Natl Acad Sci U S A       Date:  1981-03       Impact factor: 11.205
  1 in total

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