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 Stephenson, S.
Right arrow Articles by Perego, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stephenson, S.
Right arrow Articles by Perego, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2003, p. 4861-4871, Vol. 185, No. 16
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.16.4861-4871.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Molecular Analysis of Phr Peptide Processing in Bacillus subtilis{dagger}

Sophie Stephenson, Christian Mueller, Min Jiang, and Marta Perego*

Division of Cellular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037

Received 27 March 2003/ Accepted 20 May 2003

In Bacillus subtilis, an export-import pathway regulates production of the Phr pentapeptide inhibitors of Rap proteins. Processing of the Phr precursor proteins into the active pentapeptide form is a key event in the initiation of sporulation and competence development. The PhrA (ARNQT) and PhrE (SRNVT) peptides inhibit the RapA and RapE phosphatases, respectively, whose activity is directed toward the Spo0F~P intermediate response regulator of the sporulation phosphorelay. The PhrC (ERGMT) peptide inhibits the RapC protein acting on the ComA response regulator for competence with regard to DNA transformation. The structural organization of PhrA, PhrE, and PhrC suggested a role for type I signal peptidases in the processing of the Phr preinhibitor, encoded by the phr genes, into the proinhibitor form. The proinhibitor was then postulated to be cleaved to the active pentapeptide inhibitor by an additional enzyme. In this report, we provide evidence that Phr preinhibitor proteins are subject to only one processing event at the peptide bond on the amino-terminal end of the pentapeptide. This processing event is most likely independent of type I signal peptidase activity. In vivo and in vitro analyses indicate that none of the five signal peptidases of B. subtilis (SipS, SipT, SipU, SipV, and SipW) are indispensable for Phr processing. However, we show that SipV and SipT have a previously undescribed role in sporulation, competence, and cell growth.

* Corresponding author. Mailing address: Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, CA 92037. Phone: (858) 784-7912. Fax: (858) 784-7966. E-mail: mperego{at}scripps.edu.

{dagger} This is publication 15076-MEM from the Scripps Research Institute.

Journal of Bacteriology, August 2003, p. 4861-4871, Vol. 185, No. 16
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.16.4861-4871.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hamze, K., Julkowska, D., Autret, S., Hinc, K., Nagorska, K., Sekowska, A., Holland, I. B., Seror, S. J. (2009). Identification of genes required for different stages of dendritic swarming in Bacillus subtilis, with a novel role for phrC. Microbiology 155: 398-412 [Abstract] [Full Text]  
  • Lanigan-Gerdes, S., Briceno, G., Dooley, A. N., Faull, K. F., Lazazzera, B. A. (2008). Identification of Residues Important for Cleavage of the Extracellular Signaling Peptide CSF of Bacillus subtilis from Its Precursor Protein. J. Bacteriol. 190: 6668-6675 [Abstract] [Full Text]  
  • Bouillaut, L., Perchat, S., Arold, S., Zorrilla, S., Slamti, L., Henry, C., Gohar, M., Declerck, N., Lereclus, D. (2008). Molecular basis for group-specific activation of the virulence regulator PlcR by PapR heptapeptides. Nucleic Acids Res 36: 3791-3801 [Abstract] [Full Text]  
  • Auchtung, J. M., Lee, C. A., Grossman, A. D. (2006). Modulation of the ComA-Dependent Quorum Response in Bacillus subtilis by Multiple Rap Proteins and Phr Peptides.. J. Bacteriol. 188: 5273-5285 [Abstract] [Full Text]  
  • Allenby, N. E. E., O'Connor, N., Pragai, Z., Ward, A. C., Wipat, A., Harwood, C. R. (2005). Genome-Wide Transcriptional Analysis of the Phosphate Starvation Stimulon of Bacillus subtilis. J. Bacteriol. 187: 8063-8080 [Abstract] [Full Text]  
  • Qiu, R., Pei, W., Zhang, L., Lin, J., Ji, G. (2005). Identification of the Putative Staphylococcal AgrB Catalytic Residues Involving the Proteolytic Cleavage of AgrD to Generate Autoinducing Peptide. J. Biol. Chem. 280: 16695-16704 [Abstract] [Full Text]  
  • Voigt, C. A., Wolf, D. M., Arkin, A. P. (2005). The Bacillus subtilis sin Operon: An Evolvable Network Motif. Genetics 169: 1187-1202 [Abstract] [Full Text]  
  • Wu, X., Liu, D., Lee, M. H., Golden, J. W. (2004). patS Minigenes Inhibit Heterocyst Development of Anabaena sp. Strain PCC 7120. J. Bacteriol. 186: 6422-6429 [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»