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Vol. 13, No. 6, pp. 655-665, March 15, 1999
32: evidence for a built-in RNA thermosensor
1 HSP Research Institute, Kyoto Research Park, Kyoto
600-8813, Japan; 2 Institute for Protein Research, Osaka
University, Osaka 565-0871, Japan
Induction of heat shock proteins in Escherichia coli is
primarily caused by increased cellular levels of the heat shock
-factor 32 encoded by the rpoH gene. Increased
32 levels result from both enhanced synthesis and
stabilization. Previous work indicated that 32 synthesis
is induced at the translational level and is mediated by the mRNA
secondary structure formed within the 5'-coding sequence of
rpoH, including the translation initiation region. To
understand the mechanism of heat induction of 32 synthesis
further, we analyzed expression of rpoH-lacZ gene fusions with
altered stability of mRNA structure before and after heat shock. A
clear correlation was found between the stability and expression or the
extent of heat induction. Temperature-melting profiles of mRNAs with or
without mutations correlated well with the expression patterns of
fusion genes carrying the corresponding mutations in vivo. Furthermore,
temperature dependence of mRNA-30S ribosome-tRNAfMet complex formation with wild-type
or mutant mRNAs in vitro agreed well with that of the expression of
gene fusions in vivo. Our results support a novel mechanism in which
partial melting of mRNA secondary structure at high temperature
enhances ribosome entry and translational initiation without
involvement of other cellular components, that is, intrinsic mRNA
stability controls synthesis of a transcriptional regulator.
[Key Words:
rpoH; heat shock response; 32; thermosensor; translational regulation]
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