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Journal of Bacteriology, May 1999, p. 2710-2718, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Membrane-Bound Division Proteins DivIB and DivIC of
Bacillus subtilis Function Solely through Their External
Domains in both Vegetative and Sporulation Division
Vittorio L.
Katis and
R. Gerry
Wake*
Department of Biochemistry, University of
Sydney, Sydney, New South Wales 2006, Australia
Received 3 December 1998/Accepted 8 February 1999
The Bacillus subtilis membrane-bound division proteins,
DivIB and DivIC, each contain a single transmembrane segment flanked by
a short cytoplasmic N-terminal domain and a larger external C-terminal
domain. Both proteins become localized at the division site prior to
septation. Mutagenesis of both divIB and divIC
was performed whereby the sequences encoding the cytoplasmic domains were replaced by the corresponding sequence of the other gene. Finally,
the cytoplasmic-plus-transmembrane-encoding domain of each protein was
replaced by a totally foreign sequence not involved in division, that
encodes the N-terminal-plus-transmembrane domains of the
Escherichia coli TolR protein. B. subtilis
strains expressing the divIB and divIC hybrids,
in the absence of the wild-type gene, were viable when grown under
conditions in which the wild-type genes were found previously to be
essential. Furthermore, these strains were able to sporulate to near
normal levels. Thus, the cytoplasmic and transmembrane segments of
DivIB and DivIC do not appear to have any specific functions other than
to anchor these proteins correctly in the membrane. The implications of
these findings are discussed.
*
Corresponding author. Mailing address: Department of
Biochemistry, University of Sydney, Sydney, New South Wales 2006, Australia. Phone: (61-2) 9351-2504. Fax: (61-2) 9351-4726. E-mail:
G.Wake{at}biochem.usyd.edu.au.
Journal of Bacteriology, May 1999, p. 2710-2718, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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