This Article
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 Kemp, E H
Right arrow Articles by Setlow, P
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kemp, E H
Right arrow Articles by Setlow, P

 Previous Article  |  Next Article 

J Bacteriol. 1991 August; 173(15): 4646-4652

research-article

Analysis of transcriptional control of the gerD spore germination gene of Bacillus subtilis 168.

E H Kemp, R L Sammons, A Moir, D Sun and P Setlow

Krebs Institute, Department of Molecular Biology and Biotechnology, Sheffield, United Kingdom.

ABSTRACT

The gerD locus of Bacillus subtilis comprises a single gene whose function is essential for the germination of B. subtilis spores in media containing asparagine, glucose, and fructose. The expression of gerD has been characterized by using a chromosomal lacZ fusion to the gerD promoter. The promoter is switched on at the same time as the synthesis of glucose dehydrogenase, 2.5 h after sporulation has been initiated in the developing forespore. The gerD gene is not expressed in spoIIB or spoIIIA, -IIIB, -EIII, -FIII, or -IIIG mutants, but it is expressed in spoIIIC and -IIID and spoIVA mutant backgrounds. The in vivo transcriptional start point of the gene has been mapped by primer extension analysis, and sequences upstream from the start point show considerable homology with the promoter consensus sequences recognized by RNA polymerase containing the forespore-specific sigma factor sigma G (E sigma G). gerD is transcribed in vitro by E sigma G with a similar if not identical start point to that found in vivo, and expression of the gene can be rapidly induced in vegetative cells following the induction of sigma G synthesis. These results indicate that gerD is another member of the sigma G regulon, which includes a number of genes expressed only in the forespore compartment of sporulating cells of B. subtilis.

J Bacteriol. 1991 August; 173(15): 4646-4652




This article has been cited by other articles:

  • Mongkolthanaruk, W., Robinson, C., Moir, A. (2009). Localization of the GerD spore germination protein in the Bacillus subtilis spore. Microbiology 155: 1146-1151 [Abstract] [Full Text]  
  • Visai, L., Yanagisawa, N., Josefsson, E., Tarkowski, A., Pezzali, I., Rooijakkers, S. H. M., Foster, T. J., Speziale, P. (2009). Immune evasion by Staphylococcus aureus conferred by iron-regulated surface determinant protein IsdH. Microbiology 155: 667-679 [Abstract] [Full Text]  
  • Pelczar, P. L., Setlow, P. (2008). Localization of the Germination Protein GerD to the Inner Membrane in Bacillus subtilis Spores. J. Bacteriol. 190: 5635-5641 [Abstract] [Full Text]  
  • Stapleton, M. R., Horsburgh, M. J., Hayhurst, E. J., Wright, L., Jonsson, I.-M., Tarkowski, A., Kokai-Kun, J. F., Mond, J. J., Foster, S. J. (2007). Characterization of IsaA and SceD, Two Putative Lytic Transglycosylases of Staphylococcus aureus. J. Bacteriol. 189: 7316-7325 [Abstract] [Full Text]  
  • Pelczar, P. L., Igarashi, T., Setlow, B., Setlow, P. (2007). Role of GerD in Germination of Bacillus subtilis Spores. J. Bacteriol. 189: 1090-1098 [Abstract] [Full Text]  
  • Shaw, L. N., Aish, J., Davenport, J. E., Brown, M. C., Lithgow, J. K., Simmonite, K., Crossley, H., Travis, J., Potempa, J., Foster, S. J. (2006). Investigations into {sigma}B-Modulated Regulatory Pathways Governing Extracellular Virulence Determinant Production in Staphylococcus aureus.. J. Bacteriol. 188: 6070-6080 [Abstract] [Full Text]  
  • Kaatz, G. W., DeMarco, C. E., Seo, S. M. (2006). MepR, a Repressor of the Staphylococcus aureus MATE Family Multidrug Efflux Pump MepA, Is a Substrate-Responsive Regulatory Protein.. Antimicrob. Agents Chemother. 50: 1276-1281 [Abstract] [Full Text]  
  • Kaatz, G. W., McAleese, F., Seo, S. M. (2005). Multidrug Resistance in Staphylococcus aureus Due to Overexpression of a Novel Multidrug and Toxin Extrusion (MATE) Transport Protein. Antimicrob. Agents Chemother. 49: 1857-1864 [Abstract] [Full Text]  
  • Shaw, L. N., Golonka, E., Szmyd, G., Foster, S. J., Travis, J., Potempa, J. (2005). Cytoplasmic Control of Premature Activation of a Secreted Protease Zymogen: Deletion of Staphostatin B (SspC) in Staphylococcus aureus 8325-4 Yields a Profound Pleiotropic Phenotype. J. Bacteriol. 187: 1751-1762 [Abstract] [Full Text]  
  • Steil, L., Serrano, M., Henriques, A. O., Volker, U. (2005). Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis. Microbiology 151: 399-420 [Abstract] [Full Text]  
  • Kaatz, G. W., Thyagarajan, R. V., Seo, S. M. (2005). Effect of Promoter Region Mutations and mgrA Overexpression on Transcription of norA, Which Encodes a Staphylococcus aureus Multidrug Efflux Transporter. Antimicrob. Agents Chemother. 49: 161-169 [Abstract] [Full Text]  
  • Kaatz, G. W., Seo, S. M. (2004). Effect of substrate exposure and other growth condition manipulations on norA expression. J Antimicrob Chemother 54: 364-369 [Abstract] [Full Text]  
  • Horsburgh, M. J., Wiltshire, M. D., Crossley, H., Ingham, E., Foster, S. J. (2004). PheP, a Putative Amino Acid Permease of Staphylococcus aureus, Contributes to Survival In Vivo and during Starvation. Infect. Immun. 72: 3073-3076 [Abstract] [Full Text]  
  • Lithgow, J. K., Hayhurst, E. J., Cohen, G., Aharonowitz, Y., Foster, S. J. (2004). Role of a Cysteine Synthase in Staphylococcus aureus. J. Bacteriol. 186: 1579-1590 [Abstract] [Full Text]  
  • Lithgow, J. K., Ingham, E., Foster, S. J. (2004). Role of the hprT-ftsH locus in Staphylococcus aureus. Microbiology 150: 373-381 [Abstract] [Full Text]  
  • Shaw, L., Golonka, E., Potempa, J., Foster, S. J. (2004). The role and regulation of the extracellular proteases of Staphylococcus aureus. Microbiology 150: 217-228 [Abstract] [Full Text]  
  • Karavolos, M. H., Horsburgh, M. J., Ingham, E., Foster, S. J. (2003). Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology 149: 2749-2758 [Abstract] [Full Text]  
  • Clarke, S. R., Harris, L. G., Richards, R. G., Foster, S. J. (2002). Analysis of Ebh, a 1.1-Megadalton Cell Wall-Associated Fibronectin-Binding Protein of Staphylococcus aureus. Infect. Immun. 70: 6680-6687 [Abstract] [Full Text]  
  • Wiltshire, M. D., Foster, S. J. (2001). Identification and Analysis of Staphylococcus aureus Components Expressed by a Model System of Growth in Serum. Infect. Immun. 69: 5198-5202 [Abstract] [Full Text]  
  • Tjalsma, H., Kontinen, V. P., Pragai, Z., Wu, H., Meima, R., Venema, G., Bron, S., Sarvas, M., van Dijl, J. M. (1999). The Role of Lipoprotein Processing by Signal Peptidase II in the Gram-positive Eubacterium Bacillus subtilis. SIGNAL PEPTIDASE II IS REQUIRED FOR THE EFFICIENT SECRETION OF alpha -AMYLASE, A NON-LIPOPROTEIN. J. Biol. Chem. 274: 1698-1707 [Abstract] [Full Text]  
  • Chan, P. F., Foster, S. J., Ingham, E., Clements, M. O. (1998). The Staphylococcus aureus Alternative Sigma Factor sigma B Controls the Environmental Stress Response but Not Starvation Survival or Pathogenicity in a Mouse Abscess Model. J. Bacteriol. 180: 6082-6089 [Abstract] [Full Text]  
  • Chan, P. F., Foster, S. J. (1998). Role of SarA in Virulence Determinant Production and Environmental Signal Transduction in Staphylococcus aureus. J. Bacteriol. 180: 6232-6241 [Abstract] [Full Text]  
  • McAleese, F. M., Walsh, E. J., Sieprawska, M., Potempa, J., Foster, T. J. (2001). Loss of Clumping Factor B Fibrinogen Binding Activity by Staphylococcus aureus Involves Cessation of Transcription, Shedding and Cleavage by Metalloprotease. J. Biol. Chem. 276: 29969-29978 [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»