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Vol. 14, No. 9, pp. 1109-1118, May 1, 2000
Institute of Microbiology and Genetics, Vienna Biocenter,
1030 Vienna, Austria
The adaptation of mRNA stability to environmental changes is a means
of cells to adjust the level of gene expression. The Escherichia
coli ompA mRNA has served as one of the paradigms for regulated
mRNA decay in prokaryotes. The stability of the transcript is known to
be correlated inversely with the bacterial growth rate. Thus, the
regulation of ompA mRNA stability meets the physiological needs
to adjust the level of ompA expression to the rate of cell
division. Recently, host factor I (Hfq/HF1) was shown to
be involved in the regulation of ompA mRNA stability under slow
growth conditions. Here, we present the first direct demonstration that
30S ribosomes bound to the ompA 5'-UTR protect the
transcript from RNase E cleavage in vitro. However, the 30S protection
was found to be abrogated in the presence of Hfq. Toeprinting and in
vitro translation assays revealed that translation of ompA is
repressed in the presence of Hfq. These in vitro studies are corroborated by in vivo expression studies demonstrating that the
reduced synthesis rate of OmpA effected by Hfq results in functional
inactivation of the ompA mRNA. The data are discussed in terms of a
model wherein Hfq regulates the stability of ompA mRNA by
competing with 30S ribosomes for binding to the ompA 5'-UTR.
[Key Words: Hfq; mRNA stability; ompA; translation initiation]
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