Journal article
The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site
Journal of bacteriology, Vol.184(4), pp.904-912
02/2002
DOI: 10.1128/jb.184.4.904-912.2002
PMCID: PMC134820
PMID: 11807049
Abstract
The bacterial cell division protein FtsW has been suggested to perform two functions: stabilize the FtsZ cytokinetic ring, and facilitate septal peptidoglycan synthesis by the transpeptidase FtsI (penicillin-binding protein 3). We show here that depleting Escherichia coli cells of FtsW had little effect on the abundance of FtsZ rings but abrogated recruitment of FtsI to potential division sites. Analysis of FtsW localization confirmed and extended these results; septal localization of FtsW required FtsZ, FtsA, FtsQ, and FtsL but not FtsI. Thus, FtsW is a late recruit to the division site and is essential for subsequent recruitment of its cognate transpeptidase FtsI but not for stabilization of FtsZ rings. We suggest that a primary function of FtsW homologues--which are found in almost all bacteria and appear to work in conjunction with dedicated transpeptidases involved in division, elongation, or sporulation--is to recruit their cognate transpeptidases to the correct subcellular location.
Details
- Title: Subtitle
- The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site
- Creators
- Keri L N Mercer - Department of Microbiology, University of Iowa, Iowa City, Iowa 52242, USADavid S Weiss
- Resource Type
- Journal article
- Publication Details
- Journal of bacteriology, Vol.184(4), pp.904-912
- Publisher
- United States
- DOI
- 10.1128/jb.184.4.904-912.2002
- PMID
- 11807049
- PMCID
- PMC134820
- ISSN
- 0021-9193
- eISSN
- 1098-5530
- Grant note
- R01 GM059893 / NIGMS NIH HHS GM59893 / NIGMS NIH HHS
- Language
- English
- Date published
- 02/2002
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984001127802771
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