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Journal of Bacteriology, September 2004, p. 5567-5575, Vol. 186, No. 17
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.17.5567-5575.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Transglutaminase-Mediated Cross-Linking of GerQ in the Coats of Bacillus subtilis Spores
Katerina Ragkousi and Peter Setlow*
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut
Received 12 April 2004/
Accepted 27 May 2004
The spores of Bacillus subtilis show remarkable resistance to many environmental stresses, due in part to the presence of an outer proteinaceous structure known as the spore coat. GerQ is a spore coat protein essential for the presence of CwlJ, an enzyme involved in the hydrolysis of the cortex during spore germination, in the spore coat. Here we show that GerQ is cross-linked into higher-molecular-mass forms due in large part to a transglutaminase. GerQ is the only substrate for this transglutaminase identified to date. In addition, we show that cross-linking of GerQ into high-molecular-mass forms occurs only very late in sporulation, after mother cell lysis. These findings, as well as studies of GerQ cross-linking in mutant strains where spore coat assembly is perturbed, lead us to suggest that coat proteins must assemble first and that their cross-linking follows as a final step in the spore coat formation pathway.
* Corresponding author. Mailing address: Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06032. Phone: (860) 679-2607. Fax: (860) 679-3408. E-mail:
setlow{at}nso2.uchc.edu.
Journal of Bacteriology, September 2004, p. 5567-5575, Vol. 186, No. 17
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.17.5567-5575.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
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