J Bacteriol, March 1998, p. 1375-1380, Vol. 180, No. 6
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Department of Applied Biology,
Received 14 November 1997/Accepted 3 January 1998
The predicted amino acid sequence of Bacillus subtilis
ycbQ (renamed cwlJ) exhibits high similarity to those
of the deduced C-terminal catalytic domain of SleBs, the specific
cortex-hydrolyzing enzyme of B. cereus and the deduced one
of B. subtilis. We constructed a
cwlJ::lacZ fusion in the B. subtilis
chromosome. The
-galactosidase activity and results of Northern
hybridization and primer extension analyses of the cwlJ
gene indicated that it is transcribed by E
E RNA
polymerase. cwlJ-deficient spores responded to both
L-alanine and AGFK, the A580 values
of spore suspensions decreased more slowly than in the case of the
wild-type strain, and the mutant spores released less dipicolinic acid
than did those of the wild-type strain during germination. However, the
mutant spores released only slightly less hexosamine than did the
wild-type spores. In contrast, B. subtilis sleB spores did
not release hexosamine at a significant level. While cwlJ
and sleB spores were able to germinate, CJSB (cwlJ
sleB) spores could not germinate but exhibited initial germination reactions, e.g., partial decrease in
A580 and slow release of dipicolinic acid. CJSB
spores became slightly gray after 6 h in the germinant, but their
refractility was much greater than that of sleB mutant
spores. The roles of the sleB and cwlJ mutations in germination and spore maturation are also discussed.
*
Corresponding author. Mailing address: Department of
Applied Biology, Faculty of Textile Science and Technology, Shinshu
University, 3-15-1 Tokida, Ueda-shi, Nagano 386, Japan. Phone:
81-268-21-5344. Fax: 81-268-21-5331. E-mail:
jsekigu{at}giptc.shinshu-u.ac.jp.
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