This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Krajcíková, D.
Right arrow Articles by Barák, I.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Krajcíková, D.
Right arrow Articles by Barák, I.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 2009, p. 3212-3219, Vol. 191, No. 10
0021-9193/09/$08.00+0     doi:10.1128/JB.01807-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Searching for Protein-Protein Interactions within the Bacillus subtilis Spore Coat{triangledown}

Daniela Krajcíková,1 Magda Lukácová,1 Denisa Müllerová,1 Simon M. Cutting,2 and Imrich Barák1*

Institute of Molecular Biology, Slovak Academy of Sciences, Bratislava, Slovakia,1 Royal Holloway and Bedford New College, University of London, London, United Kingdom2

Received 23 December 2008/ Accepted 11 March 2009

The capability of endospores of Bacillus subtilis to withstand extreme environmental conditions is secured by several attributes. One of them, the protein shell that encases the spore and is known as the coat, provides the spore with its characteristic resistance to toxic chemicals, lytic enzymes, and predation by unicellular and multicellular eukaryotes. Despite most of the components of the spore coat having been identified, we have only a vague understanding of how such a complex structure is assembled. Using the yeast two-hybrid system, we attempted to identify direct contacts among the proteins allocated to the insoluble fraction of the spore coat: CotV, CotW, CotX, CotY, and CotZ. We also examined whether they could interact with CotE, one of the most crucial morphogenetic proteins governing outer coat formation and also present in the insoluble fraction. Out of all 21 possible interactions we tested, 4 were found to be positive. Among these interactions, we confirmed the previous observation that CotE forms homo-oligomers. In addition, we observed homotypic interactions of CotY, strong interactions between CotZ and CotY, and relatively weak, yet significant, interactions between CotV and CotW. The results of this yeast two-hybrid analysis were confirmed by size exclusion chromatography of recombinant coat proteins and a pull-down assay.

* Corresponding author. Mailing address: Institute of Molecular Biology, Slovak Academy of Sciences, Dubravska cesta 21, Bratislava 845 51, Slovakia. Phone: 421 2 5930 7418. Fax: 421 2 5930 7416. E-mail: imrich.barak{at}savba.sk

{triangledown} Published ahead of print on 20 March 2009.

Journal of Bacteriology, May 2009, p. 3212-3219, Vol. 191, No. 10
0021-9193/09/$08.00+0     doi:10.1128/JB.01807-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»