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Journal of Bacteriology, September 1998, p. 4555-4563, Vol. 180, No. 17
Department of Biochemistry, University of
Connecticut Health Center, Farmington, Connecticut 06030
Received 4 May 1998/Accepted 1 July 1998
Bacillus subtilis strains lacking
penicillin-binding protein 1 (PBP1), encoded by ponA,
required greater amounts of Mg2+ or
Ca2+ for vegetative growth or spore outgrowth than the
wild-type strain and strains lacking other high-molecular-weight (HMW)
PBPs. Growth of ponA cells in a medium low in
Mg2+ also resulted in greatly increased cell bending
compared to wild-type cells or cells lacking other HMW PBPs. The
addition of high levels of Mg2+ to growth
media eliminated these phenotypes of a ponA mutant. In
contrast to the effects of divalent cations, NaCl did not restore ponA cell growth in a divalent-cation-deficient medium.
Surprisingly, wild-type cells swelled and then lysed during both
vegetative growth and spore outgrowth when 500 mM NaCl was included in
a divalent-cation-deficient medium. Again, Mg2+ addition
was sufficient to allow normal vegetative growth and spore
outgrowth of both wild-type and ponA cells in a medium with 500 mM NaCl. These studies demonstrate that (i) while HMW PBPs possess
largely redundant functions in rich medium, when divalent cations are
limiting, PBP1 is required for cell growth and spore outgrowth; and
(ii) high levels of NaCl induce cell lysis in media deficient in
divalent cations during both vegetative growth and spore outgrowth.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Bacillus subtilis Cells Lacking Penicillin-Binding
Protein 1 Require Increased Levels of Divalent Cations for
Growth
and
*
Corresponding author. Mailing address: Department of
Biochemistry, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06030. Phone: (203) 679-2607. Fax: (203) 679-3408. E-mail: setlow{at}sun.uchc.edu.
Present address: Dept. of Biology, Virginia Polytechnic Institute
and State University, Blacksburg, VA 24061-0406.
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