Literature DB >> 7708493

Genetic selection for active E.coli amber tRNA(Asn) exclusively led to glutamine inserting suppressors.

F Martin1, G Eriani, J Reinbolt, G Dirheimer, J Gangloff.   

Abstract

Suppressor tRNAs are useful tools for determining identity elements which define recognition of tRNAs in vivo by their cognate aminoacyl-tRNA synthetases. This study was aimed at the isolation of active amber tRNA(Asn). Nineteen mutated tRNA(Asn)CUA having amber suppressor activity were selected by an in vivo genetic screen, and all exclusively inserted glutamine. From analysis of the different mutations it is concluded that glutamine accepting activity was obtained upon reducing the interaction strength between the first base pair of the tRNA(Asn)CUA by direct or indirect effects. Failure to isolate tRNA(Asn)CUA suppressors charged with asparagine as well as other evolutionary related amino acids is discussed.

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Year:  1995        PMID： 7708493      PMCID： PMC306759          DOI： 10.1093/nar/23.5.779

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


  37 in total

1.  Sequence-specific recognition of double helical nucleic acids by proteins.

Authors:  N C Seeman; J M Rosenberg; A Rich
Journal:  Proc Natl Acad Sci U S A       Date:  1976-03       Impact factor: 11.205

2.  Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase.

Authors:  M A Rould; J J Perona; T A Steitz
Journal:  Nature       Date:  1991-07-18       Impact factor: 49.962

3.  Construction of Escherichia coli amber suppressor tRNA genes. II. Synthesis of additional tRNA genes and improvement of suppressor efficiency.

Authors:  L G Kleina; J M Masson; J Normanly; J Abelson; J H Miller
Journal:  J Mol Biol       Date:  1990-06-20       Impact factor: 5.469

4.  Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.

Authors:  E Labouze; H Bedouelle
Journal:  J Mol Biol       Date:  1989-02-20       Impact factor: 5.469

5.  The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins.

Authors:  C P Lee; N Mandal; M R Dyson; U L RajBhandary
Journal:  Proc Natl Acad Sci U S A       Date:  1993-08-01       Impact factor: 11.205

6.  Substitution of the 3' terminal adenosine residue of transfer RNA in vivo.

Authors:  N B Reuven; M P Deutscher
Journal:  Proc Natl Acad Sci U S A       Date:  1993-05-15       Impact factor: 11.205

7.  The 3'-terminal end (NCCA) of tRNA determines the structure and stability of the aminoacyl acceptor stem.

Authors:  S Limmer; H P Hofmann; G Ott; M Sprinzl
Journal:  Proc Natl Acad Sci U S A       Date:  1993-07-01       Impact factor: 11.205

8.  An unusual RNA tertiary interaction has a role for the specific aminoacylation of a transfer RNA.

Authors:  Y M Hou; E Westhof; R Giegé
Journal:  Proc Natl Acad Sci U S A       Date:  1993-07-15       Impact factor: 11.205

9.  A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase.

Authors:  L A Sylvers; K C Rogers; M Shimizu; E Ohtsuka; D Söll
Journal:  Biochemistry       Date:  1993-04-20       Impact factor: 3.162

10.  Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl-tRNA synthetase: a complete identity set.

Authors:  Y Hayase; M Jahn; M J Rogers; L A Sylvers; M Koizumi; H Inoue; E Ohtsuka; D Söll
Journal:  EMBO J       Date:  1992-11       Impact factor: 11.598
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