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 Quisel, J. D.
Right arrow Articles by Grossman, A. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Quisel, J. D.
Right arrow Articles by Grossman, A. D.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2001, p. 6573-6578, Vol. 183, No. 22
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.22.6573-6578.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

In Vivo Effects of Sporulation Kinases on Mutant Spo0A Proteins in Bacillus subtilis

John D. Quisel, William F. Burkholder, and Alan D. Grossman*

Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Received 15 August 2000/Accepted 31 August 2001

The phosphorylated form of the response regulator Spo0A (Spo0A~P) is required for the initiation of sporulation in Bacillus subtilis. Phosphate is transferred to Spo0A from at least four histidine kinases (KinA, KinB, KinC, and KinD) by a phosphotransfer pathway composed of Spo0F and Spo0B. Several mutations in spo0A allow initiation of sporulation in the absence of spo0F and spo0B, but the mechanisms by which these mutations allow bypass of spo0F and spo0B are not fully understood. We measured the ability of KinA, KinB, and KinC to activate sporulation of five spo0A mutants in the absence of Spo0F and Spo0B. We also determined the effect of Spo0E, a Spo0A~P-specific phosphatase, on sporulation of strains containing the spo0A mutations. Our results indicate that several of the mutations relax the specificity of Spo0A, allowing Spo0A to obtain phosphate from a broader group of phosphodonors. In the course of these experiments, we observed medium-dependent effects on the sporulation of different mutants. This led us to identify a small molecule, acetoin, that can stimulate sporulation of some spo0A mutants.

* Corresponding author. Mailing address: Department of Biology, Building 68-530, Massachusetts Institute of Technology, Cambridge, MA 02139. Phone: (617) 253-1515. Fax: (617) 253-2643. E-mail: adg{at}mit.edu.

Journal of Bacteriology, November 2001, p. 6573-6578, Vol. 183, No. 22
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.22.6573-6578.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Busuioc, M., Mackiewicz, K., Buttaro, B. A., Piggot, P. J. (2009). Role of Intracellular Polysaccharide in Persistence of Streptococcus mutans. J. Bacteriol. 191: 7315-7322 [Abstract] [Full Text]  
  • Murray, E. J., Strauch, M. A., Stanley-Wall, N. R. (2009). {sigma}X Is Involved in Controlling Bacillus subtilis Biofilm Architecture through the AbrB Homologue Abh. J. Bacteriol. 191: 6822-6832 [Abstract] [Full Text]  
  • Zemansky, J., Kline, B. C., Woodward, J. J., Leber, J. H., Marquis, H., Portnoy, D. A. (2009). Development of a mariner-Based Transposon and Identification of Listeria monocytogenes Determinants, Including the Peptidyl-Prolyl Isomerase PrsA2, That Contribute to Its Hemolytic Phenotype. J. Bacteriol. 191: 3950-3964 [Abstract] [Full Text]  
  • Karatan, E., Watnick, P. (2009). Signals, Regulatory Networks, and Materials That Build and Break Bacterial Biofilms. Microbiol. Mol. Biol. Rev. 73: 310-347 [Abstract] [Full Text]  
  • Schirner, K., Errington, J. (2009). The Cell Wall Regulator {sigma}I Specifically Suppresses the Lethal Phenotype of mbl Mutants in Bacillus subtilis. J. Bacteriol. 191: 1404-1413 [Abstract] [Full Text]  
  • Monk, I. R., Gahan, C. G. M., Hill, C. (2008). Tools for Functional Postgenomic Analysis of Listeria monocytogenes. Appl. Environ. Microbiol. 74: 3921-3934 [Abstract] [Full Text]  
  • Chary, V. K., Xenopoulos, P., Piggot, P. J. (2007). Expression of the {sigma}F-Directed csfB Locus Prevents Premature Appearance of {sigma}G Activity during Sporulation of Bacillus subtilis. J. Bacteriol. 189: 8754-8757 [Abstract] [Full Text]  
  • Riedel, C. U., Monk, I. R., Casey, P. G., Morrissey, D., O'Sullivan, G. C., Tangney, M., Hill, C., Gahan, C. G. M. (2007). Improved Luciferase Tagging System for Listeria monocytogenes Allows Real-Time Monitoring In Vivo and In Vitro. Appl. Environ. Microbiol. 73: 3091-3094 [Abstract] [Full Text]  
  • Hunt, A., Rawlins, J. P., Thomaides, H. B., Errington, J. (2006). Functional analysis of 11 putative essential genes in Bacillus subtilis.. Microbiology 152: 2895-2907 [Abstract] [Full Text]  
  • Tadesse, S., Mascarenhas, J., Kosters, B., Hasilik, A., Graumann, P. L. (2005). Genetic interaction of the SMC complex with topoisomerase IV in Bacillus subtilis. Microbiology 151: 3729-3737 [Abstract] [Full Text]  
  • Chary, V. K., Meloni, M., Hilbert, D. W., Piggot, P. J. (2005). Control of the Expression and Compartmentalization of {sigma}G Activity during Sporulation of Bacillus subtilis by Regulators of {sigma}F and {sigma}E. J. Bacteriol. 187: 6832-6840 [Abstract] [Full Text]  
  • van Ooij, C., Eichenberger, P., Losick, R. (2004). Dynamic Patterns of Subcellular Protein Localization during Spore Coat Morphogenesis in Bacillus subtilis. J. Bacteriol. 186: 4441-4448 [Abstract] [Full Text]  
  • Volkov, A., Mascarenhas, J., Andrei-Selmer, C., Ulrich, H. D., Graumann, P. L. (2003). A Prokaryotic Condensin/Cohesin-Like Complex Can Actively Compact Chromosomes from a Single Position on the Nucleoid and Binds to DNA as a Ring-Like Structure. Mol. Cell. Biol. 23: 5638-5650 [Abstract] [Full Text]  
  • Weart, R. B., Levin, P. A. (2003). Growth Rate-Dependent Regulation of Medial FtsZ Ring Formation. J. Bacteriol. 185: 2826-2834 [Abstract] [Full Text]  
  • Stanley, N. R., Britton, R. A., Grossman, A. D., Lazazzera, B. A. (2003). Identification of Catabolite Repression as a Physiological Regulator of Biofilm Formation by Bacillus subtilis by Use of DNA Microarrays. J. Bacteriol. 185: 1951-1957 [Abstract] [Full Text]  
  • van Ooij, C., Losick, R. (2003). Subcellular Localization of a Small Sporulation Protein in Bacillus subtilis. J. Bacteriol. 185: 1391-1398 [Abstract] [Full Text]  
  • Hosoya, S., Asai, K., Ogasawara, N., Takeuchi, M., Sato, T. (2002). Mutation in yaaT Leads to Significant Inhibition of Phosphorelay during Sporulation in Bacillus subtilis. J. Bacteriol. 184: 5545-5553 [Abstract] [Full Text]  
  • Britton, R. A., Eichenberger, P., Gonzalez-Pastor, J. E., Fawcett, P., Monson, R., Losick, R., Grossman, A. D. (2002). Genome-Wide Analysis of the Stationary-Phase Sigma Factor (Sigma-H) Regulon of Bacillus subtilis. J. Bacteriol. 184: 4881-4890 [Abstract] [Full Text]  
  • Schneider, K. B., Palmer, T. M., Grossman, A. D. (2002). Characterization of comQ and comX, Two Genes Required for Production of ComX Pheromone in Bacillus subtilis. J. Bacteriol. 184: 410-419 [Abstract] [Full Text]  


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