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 Zhao, Y.
Right arrow Articles by Melville, S. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhao, Y.
Right arrow Articles by Melville, S. B.

 Previous Article  |  Next Article 

J. Bacteriol., Jan 1998, 136-142, Vol 180, No. 1
Copyright © 1998, American Society for Microbiology

Identification and characterization of sporulation-dependent promoters upstream of the enterotoxin gene (cpe) of Clostridium perfringens [In Process Citation]

Y Zhao and SB Melville
Department of Microbiology and Immunology, University of Tennessee, Memphis 38163, USA.

Three promoter sites (P1, P2, and P3) responsible for the sporulation- associated synthesis of Clostridium perfringens enterotoxin, a common cause of food poisoning in humans and animals, were identified. Nested and internal deletions of the cpe promoter region were made to narrow down the location of promoter elements. To measure the effects of the deletions on the expression of cpe, translational fusions containing the promoter deletions were made with the gusA gene of Escherichia coli, which codes for beta-glucuronidase; E. coli-C. perfringens shuttle vectors carrying the fusions were introduced into C. perfringens by electroporation. In addition, in vitro transcription assays were performed with the cpe promoter region as the DNA template for extracts made from sporulating cells. DNA sequences upstream of P1 were similar to consensus SigK-dependent promoters, while P2 and P3 were similar to consensus SigE-dependent promoters. SigE and SigK are sporulation-associated sigma factors known to be active in the mother cell compartment of sporulating cells of Bacillus subtilis, the same compartment in which enterotoxin is synthesized in C. perfringens.


This article has been cited by other articles:

  • Paredes-Sabja, D., Udompijitkul, P., Sarker, M. R. (2009). Inorganic Phosphate and Sodium Ions Are Cogerminants for Spores of Clostridium perfringens Type A Food Poisoning-Related Isolates. Appl. Environ. Microbiol. 75: 6299-6305 [Abstract] [Full Text]  
  • Paredes-Sabja, D., Setlow, P., Sarker, M. R. (2009). The protease CspB is essential for initiation of cortex hydrolysis and dipicolinic acid (DPA) release during germination of spores of Clostridium perfringens type A food poisoning isolates. Microbiology 155: 3464-3472 [Abstract] [Full Text]  
  • Paredes-Sabja, D., Setlow, P., Sarker, M. R. (2009). GerO, a Putative Na+/H+-K+ Antiporter, Is Essential for Normal Germination of Spores of the Pathogenic Bacterium Clostridium perfringens. J. Bacteriol. 191: 3822-3831 [Abstract] [Full Text]  
  • Paredes-Sabja, D., Setlow, P., Sarker, M. R. (2009). Role of GerKB in Germination and Outgrowth of Clostridium perfringens Spores. Appl. Environ. Microbiol. 75: 3813-3817 [Abstract] [Full Text]  
  • Harry, K. H., Zhou, R., Kroos, L., Melville, S. B. (2009). Sporulation and Enterotoxin (CPE) Synthesis Are Controlled by the Sporulation-Specific Sigma Factors SigE and SigK in Clostridium perfringens. J. Bacteriol. 191: 2728-2742 [Abstract] [Full Text]  
  • Paredes-Sabja, D., Setlow, P., Sarker, M. R. (2009). SleC Is Essential for Cortex Peptidoglycan Hydrolysis during Germination of Spores of the Pathogenic Bacterium Clostridium perfringens. J. Bacteriol. 191: 2711-2720 [Abstract] [Full Text]  
  • Varga, J. J., Therit, B., Melville, S. B. (2008). Type IV Pili and the CcpA Protein Are Needed for Maximal Biofilm Formation by the Gram-Positive Anaerobic Pathogen Clostridium perfringens. Infect. Immun. 76: 4944-4951 [Abstract] [Full Text]  
  • Paredes-Sabja, D., Setlow, B., Setlow, P., Sarker, M. R. (2008). Characterization of Clostridium perfringens Spores That Lack SpoVA Proteins and Dipicolinic Acid. J. Bacteriol. 190: 4648-4659 [Abstract] [Full Text]  
  • Paredes-Sabja, D., Sarker, N., Setlow, B., Setlow, P., Sarker, M. R. (2008). Roles of DacB and Spm Proteins in Clostridium perfringens Spore Resistance to Moist Heat, Chemicals, and UV Radiation. Appl. Environ. Microbiol. 74: 3730-3738 [Abstract] [Full Text]  
  • Orsburn, B., Melville, S. B., Popham, D. L. (2008). Factors Contributing to Heat Resistance of Clostridium perfringens Endospores. Appl. Environ. Microbiol. 74: 3328-3335 [Abstract] [Full Text]  
  • Sorg, J. A., Sonenshein, A. L. (2008). Bile Salts and Glycine as Cogerminants for Clostridium difficile Spores. J. Bacteriol. 190: 2505-2512 [Abstract] [Full Text]  
  • Paredes-Sabja, D., Torres, J. A., Setlow, P., Sarker, M. R. (2008). Clostridium perfringens Spore Germination: Characterization of Germinants and Their Receptors. J. Bacteriol. 190: 1190-1201 [Abstract] [Full Text]  
  • Mendez, M., Huang, I-H., Ohtani, K., Grau, R., Shimizu, T., Sarker, M. R. (2008). Carbon Catabolite Repression of Type IV Pilus-Dependent Gliding Motility in the Anaerobic Pathogen Clostridium perfringens. J. Bacteriol. 190: 48-60 [Abstract] [Full Text]  
  • Raju, D., Setlow, P., Sarker, M. R. (2007). Antisense-RNA-Mediated Decreased Synthesis of Small, Acid-Soluble Spore Proteins Leads to Decreased Resistance of Clostridium perfringens Spores to Moist Heat and UV Radiation. Appl. Environ. Microbiol. 73: 2048-2053 [Abstract] [Full Text]  
  • Joshy, L., Chaudhry, R., Dhawan, B., Das, B. K., Kumar, L., Broor, S. (2006). Enterotoxigenic Clostridium perfringens and sporadic diarrhoea: a study from an Indian tertiary care hospital.. J Med Microbiol 55: 1757-1758 [Full Text]  
  • Huang, I-H., Sarker, M. R. (2006). Complementation of a Clostridium perfringens spo0A Mutant with Wild-Type spo0A from Other Clostridium Species. Appl. Environ. Microbiol. 72: 6388-6393 [Abstract] [Full Text]  
  • Philippe, V. A., Mendez, M. B., Huang, I-H., Orsaria, L. M., Sarker, M. R., Grau, R. R. (2006). Inorganic Phosphate Induces Spore Morphogenesis and Enterotoxin Production in the Intestinal Pathogen Clostridium perfringens.. Infect. Immun. 74: 3651-3656 [Abstract] [Full Text]  
  • Mani, N., Dupuy, B., Sonenshein, A. L. (2006). Isolation of RNA Polymerase from Clostridium difficile and Characterization of Glutamate Dehydrogenase and rRNA Gene Promoters In Vitro and In Vivo. J. Bacteriol. 188: 96-102 [Abstract] [Full Text]  
  • Raju, D., Sarker, M. R. (2005). Comparison of the Levels of Heat Resistance of Wild-Type, cpe Knockout, and cpe Plasmid-Cured Clostridium perfringens Type A Strains. Appl. Environ. Microbiol. 71: 7618-7620 [Abstract] [Full Text]  
  • Varga, J., Stirewalt, V. L., Melville, S. B. (2004). The CcpA Protein Is Necessary for Efficient Sporulation and Enterotoxin Gene (cpe) Regulation in Clostridium perfringens. J. Bacteriol. 186: 5221-5229 [Abstract] [Full Text]  
  • Hilbert, D. W., Piggot, P. J. (2004). Compartmentalization of Gene Expression during Bacillus subtilis Spore Formation. Microbiol. Mol. Biol. Rev. 68: 234-262 [Abstract] [Full Text]  
  • Feustel, L., Nakotte, S., Durre, P. (2004). Characterization and Development of Two Reporter Gene Systems for Clostridium acetobutylicum. Appl. Environ. Microbiol. 70: 798-803 [Abstract] [Full Text]  
  • Karlsson, S., Dupuy, B., Mukherjee, K., Norin, E., Burman, L. G., Akerlund, T. (2003). Expression of Clostridium difficile Toxins A and B and Their Sigma Factor TcdD Is Controlled by Temperature. Infect. Immun. 71: 1784-1793 [Abstract] [Full Text]  
  • Mani, N., Lyras, D., Barroso, L., Howarth, P., Wilkins, T., Rood, J. I., Sonenshein, A. L., Dupuy, B. (2002). Environmental Response and Autoregulation of Clostridium difficile TxeR, a Sigma Factor for Toxin Gene Expression. J. Bacteriol. 184: 5971-5978 [Abstract] [Full Text]  
  • Zimmer, M., Scherer, S., Loessner, M. J. (2002). Genomic Analysis of Clostridium perfringens Bacteriophage {phi}3626, Which Integrates into guaA and Possibly Affects Sporulation. J. Bacteriol. 184: 4359-4368 [Abstract] [Full Text]  
  • Miyamoto, K., Chakrabarti, G., Morino, Y., McClane, B. A. (2002). Organization of the Plasmid cpe Locus in Clostridium perfringens Type A Isolates. Infect. Immun. 70: 4261-4272 [Abstract] [Full Text]  
  • Mani, N., Dupuy, B. (2001). Regulation of toxin synthesis in Clostridium difficile by an alternative RNA polymerase sigma factor. Proc. Natl. Acad. Sci. USA 10.1073/pnas.101126598v1 [Abstract] [Full Text]  
  • Arcuri, E. F., Wiedmann, M., Boor, K. J. (2000). Phylogeny and functional conservation of {sigma}E in endospore-forming bacteria. Microbiology 146: 1593-1603 [Abstract] [Full Text]  
  • Wells, J. E., Hylemon, P. B. (2000). Identification and Characterization of a Bile Acid 7alpha -Dehydroxylation Operon in Clostridium sp. Strain TO-931, a Highly Active 7alpha -Dehydroxylating Strain Isolated from Human Feces. Appl. Environ. Microbiol. 66: 1107-1113 [Abstract] [Full Text]  
  • Walters, D. M., Stirewalt, V. L., Melville, S. B. (1999). Cloning, Sequence, and Transcriptional Regulation of the Operon Encoding a Putative N-Acetylmannosamine-6-Phosphate Epimerase (nanE) and Sialic Acid Lyase (nanA) in Clostridium perfringens. J. Bacteriol. 181: 4526-4532 [Abstract] [Full Text]  
  • Billington, S. J., Wieckowski, E. U., Sarker, M. R., Bueschel, D., Songer, J. G., McClane, B. A. (1998). Clostridium perfringens Type E Animal Enteritis Isolates with Highly Conserved, Silent Enterotoxin Gene Sequences. Infect. Immun. 66: 4531-4536 [Abstract] [Full Text]  
  • Mani, N., Dupuy, B. (2001). Regulation of toxin synthesis in Clostridium difficile by an alternative RNA polymerase sigma factor. Proc. Natl. Acad. Sci. USA 98: 5844-5849 [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»