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Journal of Bacteriology, April 2001, p. 2662-2666, Vol. 183, No. 8
Department of Biochemistry, University of
Connecticut Health Center, Farmington, Connecticut 06030
Received 31 October 2000/Accepted 26 January 2001
A derivative of SspC, a minor
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.8.2662-2666.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
An
/
-Type, Small, Acid-Soluble Spore Protein
Which Has Very High Affinity for DNA Prevents Outgrowth of
Bacillus subtilis Spores
and
/
-type, small, acid-soluble
spore protein (SASP) from Bacillus subtilis, was generated
that has a very high affinity for DNA. This protein
(SspC
11-D13K) was able to confer UV resistance on spores
lacking
/
-type SASP, and spores with SspC
11-D13K
triggered germination normally. However, SspC
11-D13K
blocked outgrowth of
90% of germinated spores, and
SspC
11-D13K persisted in these germinated spores,
whereas wild-type SspC was almost completely degraded. The outgrowth
phenotype of spores with SspC
11-D13K is proposed to be
due to the high stability of the SspC
11-D13K-DNA
complex, which prevents rapid degradation of this
/
-type SASP
early in germination. The persistence of this protein on spore DNA then
interferes with transcription during spore outgrowth.
*
Corresponding author. Mailing address: Department of
Biochemistry, University of Connecticut Health Center, Farmington, CT 06030. Phone: (860) 679-2607. Fax: (860) 679-3408. E-mail:
setlow{at}sun.uchc.edu.
Present address: Department of Biology, Massachusetts Institute of
Technology, Cambridge, MA 02139.
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