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 Stöver, A. G.
Right arrow Articles by Driks, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stöver, A. G.
Right arrow Articles by Driks, A.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 1999, p. 7065-7069, Vol. 181, No. 22
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Control of Synthesis and Secretion of the Bacillus subtilis Protein YqxM

Axel G. Stöver and Adam Driks*

Department of Microbiology and Immunology, Loyola University Medical Center, Maywood, Illinois 60153

Received 31 March 1999/Accepted 3 September 1999

yqxM is a Bacillus subtilis gene of unknown function residing in an operon with sipW, which encodes a signal peptidase, and tasA, which encodes an antibiotic protein secreted in a sipW-dependent manner. YqxM was undetectable during growth in a variety of rich media, including Luria-Bertani (LB) medium, or in minimal media or under heat shock or ethanol stress conditions but was synthesized and secreted during growth in LB medium supplemented with 1.2 M NaCl. Consistent with the possible involvement of sipW in YqxM secretion, inactivation of sipW prevented YqxM secretion. YqxM was produced and secreted in a sipW-dependent manner during growth in LB medium when the sequences upstream of yqxM were replaced with those of the inducible Pspac promoter. Coexpression of yqxM and sipW in Escherichia coli resulted in a decrease in the apparent molecular mass of YqxM, consistent with the removal of a signal peptide. These experiments suggest that YqxM production is induced by a high concentration of salt and that YqxM is secreted under the control of SipW. We hypothesize that during most conditions of growth, YqxM is present at very low levels or is not synthesized at all and that this low level or absence is due, at least in part, to posttranscriptional repression.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153. Phone: (708) 216-3706. Fax: (708) 216-9574. E-mail: adriks{at}luc.edu.

Journal of Bacteriology, November 1999, p. 7065-7069, Vol. 181, No. 22
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Winkelman, J. T., Blair, K. M., Kearns, D. B. (2009). RemA (YlzA) and RemB (YaaB) Regulate Extracellular Matrix Operon Expression and Biofilm Formation in Bacillus subtilis. J. Bacteriol. 191: 3981-3991 [Abstract] [Full Text]  
  • Branda, S. S., Gonzalez-Pastor, J. E., Dervyn, E., Ehrlich, S. D., Losick, R., Kolter, R. (2004). Genes Involved in Formation of Structured Multicellular Communities by Bacillus subtilis. J. Bacteriol. 186: 3970-3979 [Abstract] [Full Text]  
  • Rhee, K.-J., Sethupathi, P., Driks, A., Lanning, D. K., Knight, K. L. (2004). Role of Commensal Bacteria in Development of Gut-Associated Lymphoid Tissues and Preimmune Antibody Repertoire. J. Immunol. 172: 1118-1124 [Abstract] [Full Text]  
  • Stephenson, S., Mueller, C., Jiang, M., Perego, M. (2003). Molecular Analysis of Phr Peptide Processing in Bacillus subtilis. J. Bacteriol. 185: 4861-4871 [Abstract] [Full Text]  
  • Palacin, A., Parro, V., Geukens, N., Anne, J., Mellado, R. P. (2002). SipY Is the Streptomyces lividans Type I Signal Peptidase Exerting a Major Effect on Protein Secretion. J. Bacteriol. 184: 4875-4880 [Abstract] [Full Text]  
  • van Roosmalen, M. L., Jongbloed, J. D. H., Jong, A. d., van Eerden, J., Venema, G., Bron, S., Maarten van Dijl, J. (2001). Detergent-independent in vitro activity of a truncated Bacillus signal peptidase. Microbiology 147: 909-917 [Abstract] [Full Text]  
  • Catalano, F. A., Meador-Parton, J., Popham, D. L., Driks, A. (2001). Amino Acids in the Bacillus subtilis Morphogenetic Protein SpoIVA with Roles in Spore Coat and Cortex Formation. J. Bacteriol. 183: 1645-1654 [Abstract] [Full Text]  
  • Tjalsma, H., Bolhuis, A., Jongbloed, J. D. H., Bron, S., van Dijl, J. M. (2000). Signal Peptide-Dependent Protein Transport in Bacillus subtilis: a Genome-Based Survey of the Secretome. Microbiol. Mol. Biol. Rev. 64: 515-547 [Abstract] [Full Text]  
  • Tjalsma, H., Stover, A. G., Driks, A., Venema, G., Bron, S., van Dijl, J. M. (2000). Conserved Serine and Histidine Residues Are Critical for Activity of the ER-type Signal Peptidase SipW of Bacillus subtilis. J. Biol. Chem. 275: 25102-25108 [Abstract] [Full Text]  
  • van Roosmalen, M. L., Jongbloed, J. D. H., Dubois, J.-Y. F., Venema, G., Bron, S., van Dijl, J. M. (2001). Distinction between Major and Minor Bacillus Signal Peptidases Based on Phylogenetic and Structural Criteria. J. Biol. Chem. 276: 25230-25235 [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»