Literature DB >> 1438273

The anticodon triplet is not sufficient to confer methionine acceptance to a transfer RNA.

B Senger1, L Despons, P Walter, F Fasiolo.   

Abstract

Previous work suggested that the presence of the anticodon CAU alone was enough to confer methionine acceptance to a tRNA. Conversions of Escherichia coli nonmethionine tRNAs to a methionine-accepting species were obtained by substitutions reconstructing the whole methionine anticodon loop together with preservation (or introduction) of the acceptor stem base A73. We show here that the CAU triplet alone is unable to confer methionine acceptance when transplanted into a yeast aspartic tRNA. Both non-anticodon bases of the anticodon loop of yeast tRNA(Met) and A73 are required in addition to CAU for methionine acceptance. The importance of these non-anticodon bases in other CAU-containing tRNA frameworks was also established. These specific non-anticodon base interactions make a substantial thermodynamic contribution to the methionine acceptance of a transfer RNA.

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Year:  1992        PMID： 1438273      PMCID： PMC50423          DOI： 10.1073/pnas.89.22.10768

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  24 in total

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Authors:  P Schimmel
Journal:  Biochemistry       Date:  1989-04-04       Impact factor: 3.162

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Authors:  S A Martinis; P Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  1992-01-01       Impact factor: 11.205

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Authors:  L H Schulman
Journal:  Prog Nucleic Acid Res Mol Biol       Date:  1991

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Authors:  M Yarus
Journal:  Cell       Date:  1988-12-02       Impact factor: 41.582

5.  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 6.  Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs.

Authors:  P Schimmel
Journal:  Annu Rev Biochem       Date:  1987       Impact factor: 23.643

7.  tRNAi(met) functions in directing the scanning ribosome to the start site of translation.

Authors:  A M Cigan; L Feng; T F Donahue
Journal:  Science       Date:  1988-10-07       Impact factor: 47.728

8.  Arginine-395 is required for efficient in vivo and in vitro aminoacylation of tRNAs by Escherichia coli methionyl-tRNA synthetase.

Authors:  G Ghosh; H Y Kim; J P Demaret; S Brunie; L H Schulman
Journal:  Biochemistry       Date:  1991-12-24       Impact factor: 3.162

9.  Base substitutions in the wobble position of the anticodon inhibit aminoacylation of E. coli tRNAfMet by E. coli Met-tRNA synthetase.

Authors:  L H Schulman; H Pelka; M Susani
Journal:  Nucleic Acids Res       Date:  1983-03-11       Impact factor: 16.971

10.  Anticodon loop size and sequence requirements for recognition of formylmethionine tRNA by methionyl-tRNA synthetase.

Authors:  L H Schulman; H Pelka
Journal:  Proc Natl Acad Sci U S A       Date:  1983-11       Impact factor: 11.205
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  24 in total

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4.  Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant.

Authors:  K Wakasugi; C L Quinn; N Tao; P Schimmel
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5.  Aminoacylation identity switch of turnip yellow mosaic virus RNA from valine to methionine results in an infectious virus.

Authors:  T W Dreher; C H Tsai; J M Skuzeski
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Review 6.  Interplay of tRNA-like structures from plant viral RNAs with partners of the translation and replication machineries.

Authors:  R Giegé
Journal:  Proc Natl Acad Sci U S A       Date:  1996-10-29       Impact factor: 11.205

7.  The bipartite structure of the tRNA m1A58 methyltransferase from S. cerevisiae is conserved in humans.

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8.  The RNA helicase Mtr4p modulates polyadenylation in the TRAMP complex.

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9.  The yeast Ty3 retrotransposon contains a 5'-3' bipartite primer-binding site and encodes nucleocapsid protein NCp9 functionally homologous to HIV-1 NCp7.

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10.  Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p.

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