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Functional compensation of a recognition-defective transfer RNA by a distal base pair substitution

Academic Article
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Overview

authors

  • Hou, Y. M.
  • Schimmel, Paul

publication date

  • October 1992

journal

  • Biochemistry  Journal

abstract

  • A single G3:U70 base pair in the acceptor helix is the major determinant of alanine acceptance in alanine transfer RNAs. Transfer of this base pair into other transfer RNAs confers alanine acceptance. A G3:C70 substitution eliminates alanine acceptance in vivo and in vitro. In this work, a population of mutagenized G3:C70 alanine tRNA amber suppressors was subjected to a selection for mutations that compensate for the inactivating G3:C70 substitution. No compensatory mutations located in the acceptor helix were obtained. Instead, a U27:U43 substitution that replaced the wild-type C27:G43 in the anticodon stem created a U27:U43/G3:C70 mutant alanine tRNA that inserts alanine at amber codons in vivo. The U27:U43 substitution is at a location where previous footprinting work established an RNA-protein contact. Thus, this mutation may act by functionally coupling a distal part of the tRNA structure to the active site.

subject areas

  • Amino Acid Sequence
  • Anticodon
  • Base Composition
  • Base Sequence
  • Codon
  • Escherichia coli
  • Genes, Synthetic
  • Kinetics
  • Molecular Sequence Data
  • Mutagenesis
  • Nucleic Acid Conformation
  • Phenotype
  • RNA, Transfer, Ala
  • Suppression, Genetic
  • Tetrahydrofolate Dehydrogenase
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00157a019

PubMed ID

  • 1420150
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Additional Document Info

start page

  • 10310

end page

  • 10314

volume

  • 31

issue

  • 42

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