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Journal of Bacteriology, August 1999, p. 4986-4994, Vol. 181, No. 16
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Characterization of the yrbA Gene of
Bacillus subtilis, Involved in Resistance and Germination
of Spores
Hiromu
Takamatsu,1
Takeko
Kodama,1
Tatsuo
Nakayama,2 and
Kazuhito
Watabe1,*
Faculty of Pharmaceutical Sciences, Setsunan
University, Osaka,1 and Department of
Biochemistry, Miyazaki Medical College,
Miyazaki,2 Japan
Received 28 December 1998/Accepted 1 June 1999
Insertional inactivation of the yrbA gene of
Bacillus subtilis reduced the resistance of the mutant
spores to lysozyme. The yrbA mutant spores lost their
optical density at the same rate as the wild-type spores upon
incubation with L-alanine but became only phase gray and
did not swell. The response of the mutant spores to a combination of
asparagine, glucose, fructose, and KCl was also extremely poor; in this
medium yrbA spores exhibited only a small loss in optical
density and gave a mixture of phase-bright, -gray, and -dark spores.
Northern blot analysis of yrbA transcripts in various
sig mutants indicated that yrbA was transcribed
by RNA polymerase with
E beginning at 2 h after the
start of sporulation. The yrbA promoter was localized by
primer extension analysis, and the sequences of the
35 (TCATAAC)
and
10 (CATATGT) regions were similar to the
consensus sequences of genes recognized by
E. Sodium
dodecyl sulfate-polyacrylamide gel electrophoresis analysis of proteins
solubilized from intact yrbA mutant spores showed an
alteration in the protein profile, as 31- and 36-kDa proteins, identified as YrbA and CotG, respectively, were absent, along with some
other minor changes. Electron microscopic examination of
yrbA spores revealed changes in the spore coat, including a reduction in the density and thickness of the outer layer and the
appearance of an inner coat layer-like structure around the outside of
the coat. This abnormal coat structure was also observed on the outside
of the developing forespores of the yrbA mutant. These
results suggest that YrbA is involved in assembly of some coat proteins
which have roles in both spore lysozyme resistance and germination.
*
Corresponding author. Mailing address: Faculty of
Pharmaceutical Sciences, Setsunan University, Hirakata, Osaka 573-0101, Japan. Phone and fax: (81) 720-66-3112 or -3114. E-mail:
watabe{at}pharm.setsunan.ac.jp.
Journal of Bacteriology, August 1999, p. 4986-4994, Vol. 181, No. 16
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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