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Journal of Bacteriology, November 1999, p. 7065-7069, Vol. 181, No. 22
Department of Microbiology and Immunology,
Loyola University Medical Center, Maywood, Illinois 60153
Received 31 March 1999/Accepted 3 September 1999
yqxM is a Bacillus subtilis gene of unknown
function residing in an operon with sipW, which encodes a
signal peptidase, and tasA, which encodes an antibiotic
protein secreted in a sipW-dependent manner. YqxM was
undetectable during growth in a variety of rich media, including
Luria-Bertani (LB) medium, or in minimal media or under heat shock or
ethanol stress conditions but was synthesized and secreted during
growth in LB medium supplemented with 1.2 M NaCl. Consistent with the
possible involvement of sipW in YqxM secretion,
inactivation of sipW prevented YqxM secretion. YqxM was
produced and secreted in a sipW-dependent manner during
growth in LB medium when the sequences upstream of yqxM
were replaced with those of the inducible Pspac
promoter. Coexpression of yqxM and sipW in
Escherichia coli resulted in a decrease in the apparent
molecular mass of YqxM, consistent with the removal of a signal
peptide. These experiments suggest that YqxM production is induced by a
high concentration of salt and that YqxM is secreted under the control
of SipW. We hypothesize that during most conditions of growth, YqxM is
present at very low levels or is not synthesized at all and that this
low level or absence is due, at least in part, to posttranscriptional repression.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Control of Synthesis and Secretion of the Bacillus
subtilis Protein YqxM
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153. Phone: (708) 216-3706. Fax: (708) 216-9574. E-mail: adriks{at}luc.edu.
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