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Discrimination between glutaminyl-tRNA synthetase and seryl-tRNA synthetase involves nucleotides in the acceptor helix of tRNA.
Rogers, M J; Söll, D.
Afiliação
  • Rogers MJ; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Proc Natl Acad Sci U S A ; 85(18): 6627-31, 1988 Sep.
Article em En | MEDLINE | ID: mdl-3045821
ABSTRACT
Analysis of the in vivo amber suppressor activity of mutants derived from two Escherichia coli serine tRNAs shows that substitution of 2 base pairs in the acceptor helix changes a serine suppressor tRNA to an efficient glutamine acceptor. Determination of the amino acid inserted in vivo into protein by this tRNA shows that these changes reduce the tRNA recognition by seryl-tRNA synthetase while increasing that of glutaminyl-tRNA synthetase. This implies that misaminoacylation in vivo is dependent on the competition by different synthetases for the tRNA. In addition, the "translational efficiency" of tRNA is an integral part in observing misaminoacylation in vivo.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Serina-tRNA Ligase / Aminoacil-tRNA Sintetases / Glutamato-tRNA Ligase / Conformação de Ácido Nucleico Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 1988 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Serina-tRNA Ligase / Aminoacil-tRNA Sintetases / Glutamato-tRNA Ligase / Conformação de Ácido Nucleico Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 1988 Tipo de documento: Article