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Multiple interactions between the transmembrane division proteins of Bacillus subtilis and the role of FtsL instability in divisome assembly

Lookup NU author(s): Dr Richard Daniel, Professor Jeff Errington

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Abstract

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. Copyright © 2006, American Society for Microbiology. All Rights Reserved.


Publication metadata

Author(s): Daniel RA, Noirot-Gros M-F, Noirot P, Errington J

Publication type: Article

Publication status: Published

Journal: Journal of Bacteriology

Year: 2006

Volume: 188

Issue: 21

Pages: 7396-7404

Print publication date: 01/11/2006

ISSN (print): 0021-9193

ISSN (electronic): 1067-8832

Publisher: American Society for Microbiology

URL: http://dx.doi.org/10.1128/JB.01031-06

DOI: 10.1128/JB.01031-06

PubMed id: 16936019


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