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Exogenously provided glycine betaine can efficiently protect Bacillus subtilis from the detrimental effects of high
osmolarity environments. Through functional complementation of an Escherichia coli mutant deficient in glycine betaine uptake
with a gene library from B. subtilis, we have identified a
multicomponent glycine betaine transport system, OpuA. Uptake of
radiolabeled glycine betaine in B. subtilis was found to be
osmotically stimulated and was strongly decreased in a mutant strain
lacking the OpuA transport system. DNA sequence analysis revealed that
the components of the OpuA system are encoded by an operon (opuA) comprising three structural genes: opuAA, opuAB, and opuAC. The products of these genes exhibit
features characteristic for binding protein-dependent transport systems
and in particular show homology to the glycine betaine uptake system
ProU from E. coli. Expression of the opuA operon is
under osmotic control. The transcriptional initiation sites of opuA were mapped by high resolution primer extension analysis, and two opuA mRNAs were detected that differed by 38 base pairs at
their 5` ends. Synthesis of the shorter transcript was strongly
increased in cells grown at high osmolarity, whereas the amount of the
longer transcript did not vary in response to medium osmolarity.
Physical and genetic mapping experiments allowed the positioning the opuA operon at 25° on the genetic map of B.
subtilis.
Volume 270,
Number 28,
Issue of July 14, pp. 16701-16713, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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