Open AccessWhen Starting Over Makes More Sense
Author(s) -
Scott C. Blanchard
Publication year - 2009
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/cb900030w
Subject(s) - proofreading , ribosome , fidelity , translation (biology) , dna , rna , substrate (aquarium) , release factor , mechanism (biology) , biophysics , chemistry , biology , computational biology , microbiology and biotechnology , biochemistry , messenger rna , polymerase , computer science , physics , gene , telecommunications , ecology , quantum mechanics
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.