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Overview

MeSH

  • Aminoacylation
  • Base Pair Mismatch
  • Biocatalysis
  • Models, Biological
  • Models, Molecular
  • Peptide Termination Factors
  • RNA, Transfer
  • Substrate Specificity

MeSH Major

  • Peptide Chain Termination, Translational
  • Ribosomes

abstract

  • Proofreading mechanisms intrinsic to DNA and RNA polymers that contribute substantially to overall fidelity are lacking in the ribosome. New evidence, however, suggests that quality control in translation can occur after substrate incorporation by an abortive mechanism entailing premature release factor-catalyzed termination. These data shed new light on the importance and ubiquity of retrospective quality control mechanisms in ensuring the overall fidelity of nature's processive enzymes and demonstrate that competitive elongation reactions on the ribosome are kinetically sensitive to compositional features of the translating particle.

publication date

  • February 20, 2009

has subject area

  • Aminoacylation
  • Base Pair Mismatch
  • Biocatalysis
  • Models, Biological
  • Models, Molecular
  • Peptide Chain Termination, Translational
  • Peptide Termination Factors
  • RNA, Transfer
  • Ribosomes
  • Substrate Specificity

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3433159

Digital Object Identifier (DOI)

  • 10.1021/cb900030w

PubMed ID

  • 19228069

Additional Document Info

start page

  • 89

end page

  • 92

volume

  • 4

number

  • 2