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J Biol Chem, Vol. 275, Issue 18, 13849-13855, May 5, 2000
From the Department of Biochemistry, Michigan State University,
East Lansing, Michigan 48824
During sporulation of Bacillus
subtilis, spore coat proteins encoded by cot genes
are expressed in the mother cell and deposited on the forespore.
Transcription of the cotB, cotC, and
cotX genes by
Combined Action of Two Transcription Factors Regulates Genes
Encoding Spore Coat Proteins of Bacillus subtilis*
K RNA polymerase is activated
by a small, DNA-binding protein called GerE. The promoter region of
each of these genes has two GerE binding sites. 5' deletions that
eliminated the more upstream GerE site decreased expression of
lacZ fused to cotB and cotX by
approximately 80% and 60%, respectively but had no effect on cotC-lacZ expression. The
cotC-lacZ fusion was expressed later during
sporulation than the other two fusions. Primer extension analysis
confirmed that cotB mRNA increases first during
sporulation, followed by cotX and cotC
mRNAs over a 2-h period. In vitro transcription experiments suggest that the differential pattern of cot
gene expression results from the combined action of GerE and another transcription factor, SpoIIID. A low concentration of GerE activated cotB transcription by K RNA polymerase,
whereas a higher concentration was needed to activate transcription of
cotX or cotC. SpoIIID at low concentration repressed cotC transcription, whereas a higher
concentration only partially repressed cotX transcription
and had little effect on cotB transcription. DNase I
footprinting showed that SpoIIID binds strongly to two sites in the
cotC promoter region, binds weakly to one site in the
cotX promoter, and does not bind specifically to
cotB. We propose that late in sporulation the rising level of GerE and the falling level of SpoIIID, together with the position and affinity of binding sites for these transcription factors in
cot gene promoters, dictates the timing and level of spore coat protein synthesis, ensuring optimal assembly of the protein shell
on the forespore surface.
*
This research was supported by National Institutes of Health
Grant GM43585 and by the Michigan Agricultural Experiment Station.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biochemistry,
Michigan State University, East Lansing, MI 48824. Tel.: 517-355-9726;
Fax: 517-353-9334; E-mail: kroos@pilot.msu.edu.
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