JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
JB.01031-06v1
188/21/7396    most recent
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 Daniel, R. A.
Right arrow Articles by Errington, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Daniel, R. A.
Right arrow Articles by Errington, J.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2006, p. 7396-7404, Vol. 188, No. 21
0021-9193/06/$08.00+0     doi:10.1128/JB.01031-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Multiple Interactions between the Transmembrane Division Proteins of Bacillus subtilis and the Role of FtsL Instability in Divisome Assembly{triangledown}

Richard A. Daniel,1* Marie-Françoise Noirot-Gros,2 Philippe Noirot,2 and Jeff Errington1

Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom,1 Laboratoire de Génétique Microbienne, Domaine de Vilvert, INRA, 78352 Jouy en Josas Cedex, France2

Received 13 July 2006/ Accepted 5 August 2006

About 11 essential proteins assemble into a ring structure at the surface of the cell to bring about cytokinesis in bacteria. Several of these proteins have their major domains located outside the membrane, forming an assembly that we call the outer ring (OR). Previous work on division in Bacillus subtilis has shown that four of the OR proteins—FtsL, DivIC, DivIB, and PBP 2B—are interdependent for assembly. This contrasts with the mainly linear pathway for the equivalent proteins in Escherichia coli. Here we show that the interdependent nature of the B. subtilis pathway could be due to effects on FtsL and DivIC stability and that DivIB is an important player in regulating this turnover. Two-hybrid approaches suggest that a multiplicity of protein-protein interactions contribute to the assembly of the OR. DivIC is unusual in interacting strongly only with FtsL. We propose a model for the formation of the OR through the mutual association of the membrane proteins directed by the cytosolic inner-ring proteins.


* Corresponding author. Mailing address: Institute for Cell and Molecular Biosciences, Medical School, Newcastle University, Catherine Cookson Building, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom. Phone: 0191 2228866. Fax: 0191 2227424. E-mail: Richard.Daniel{at}ncl.ac.uk.

{triangledown} Published ahead of print on 25 August 2006.


Journal of Bacteriology, November 2006, p. 7396-7404, Vol. 188, No. 21
0021-9193/06/$08.00+0     doi:10.1128/JB.01031-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2006 by the American Society for Microbiology. All rights reserved.