JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wade, K. H.
Right arrow Articles by Moran, C. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wade, K. H.
Right arrow Articles by Moran, C. P., Jr.

 Previous Article  |  Next Article 

Journal of Bacteriology, July 1999, p. 4365-4373, Vol. 181, No. 14
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

A Region of sigma K Involved in Promoter Activation by GerE in Bacillus subtilis

Kathryn H. Wade, Ghislain Schyns, Jason A. Opdyke, and Charles P. Moran Jr.*

Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322

Received 3 March 1999/Accepted 7 May 1999

During endospore formation in Bacillus subtilis, the DNA binding protein GerE stimulates transcription from several promoters that are used by RNA polymerase containing sigma K. GerE binds to a site on one of these promoters, cotX, that overlaps its -35 region. We tested the model that GerE interacts with sigma K at the cotX promoter by seeking amino acid substitutions in sigma K that interfered with GerE-dependent activation of the cotX promoter but which did not affect utilization of the sigma K-dependent, GerE-independent promoter gerE. We identified two amino acid substitutions in sigma K, E216K and H225Y, that decrease cotX promoter utilization but do not affect gerE promoter activity. Alanine substitutions at these positions had similar effects. We also examined the effects of the E216A and H225Y substitutions in sigma K on transcription in vitro. We found that these substitutions specifically reduced utilization of the cotX promoter. These and other results suggest that the amino acid residues at positions 216 and 225 are required for GerE-dependent cotX promoter activity, that the histidine at position 225 of sigma K may interact with GerE at the cotX promoter, and that this interaction may facilitate the initial binding of sigma K RNA polymerase to the cotX promoter. We also found that the alanine substitutions at positions 216 and 225 of sigma K had no effect on utilization of the GerE-dependent promoter cotD, which contains GerE binding sites that do not overlap with its -35 region.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322. Phone: (404) 727-5969. Fax: (404) 727-3659. E-mail: moran{at}microbio.emory.edu.

Journal of Bacteriology, July 1999, p. 4365-4373, Vol. 181, No. 14
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1999 by the American Society for Microbiology. All rights reserved.