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Two protein release factors (RFs) showing codon specificity,
RF-1 (UAG, UAA) and RF-2 (UAA, UGA), are required for polypeptide chain
termination in Escherichia coli. We recently reported the
localization and characterization of the gene encoding RF-3
( prfC), a third protein component previously described as
stimulating termination without codon specificity. RF-3 is a
GTP-binding protein that displays much sequence similarity to
elongation factor EF-G. In a termination assay in vitro, RF-3
lowers the K
Volume 270,
Number 18,
Issue of May 5, pp. 10595-10600, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
RF-3 ACTION IN TERMINATION IS PREDOMINANTLY AT UGA-CONTAINING
STOP SIGNALS
for terminator
trinucleotides and is thought to act in termination signal recognition.
The gene prfC was identified by transposon insertion
mutagenesis leading to enhanced nonsense suppression of UGA. We report
here that (i) RF-3 inactivation significantly enhances the suppression
of termination in vivo only at UGA-dependent stop signals;
(ii) the codon-dependent contribution to the stimulation of fMet
release in vitro by RF-3 is significantly greater with UGA
termination triplet than UAG termination triplet; (iii) RF-3 increases
dramatically the affinity of RF-2 to the UGA termination complex in
vitro but not that of RF-1 to the UAG termination complex; (iv)
RF-3 inactivation leads to a positive feedback on the autoregulation of
RF-2 synthesis in vivo, dependent on the competition between
frameshifting and termination. These findings are discussed in terms of
the mechanism of involvement of RF-3 in translation termination.
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