Browse by author
Lookup NU author(s): Dr Richard Daniel,
Professor Jeff Errington FRSORCiD
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
Author(s): Daniel RA, Noirot-Gros M-F, Noirot P, Errington J
Publication type: Article
Publication status: Published
Journal: Journal of Bacteriology
Print publication date: 01/11/2006
ISSN (print): 0021-9193
ISSN (electronic): 1067-8832
Publisher: American Society for Microbiology
PubMed id: 16936019
Altmetrics provided by Altmetric