Journal article
Localization of FtsI (PBP3) to the Septal Ring Requires Its Membrane Anchor, the Z Ring, FtsA, FtsQ, and FtsL
Journal of bacteriology, Vol.181(2), pp.508-520
01/1999
DOI: 10.1128/jb.181.2.508-520.1999
PMCID: PMC93405
PMID: 9882665
Abstract
Assembly of the division septum in bacteria is mediated by several proteins that localize to the division site. One of these, FtsI (also called penicillin-binding protein 3) of
Escherichia coli
, consists of a short cytoplasmic domain, a single membrane-spanning segment, and a large periplasmic domain that encodes a transpeptidase activity involved in synthesis of septal peptidoglycan. We have constructed a merodiploid strain with a wild-type copy of
ftsI
at the normal chromosomal locus and a genetic fusion of
ftsI
to the green fluorescent protein (
gfp
) at the lambda attachment site.
gfp-ftsI
was expressed at physiologically appropriate levels under control of a regulatable promoter. Consistent with previous results based on immunofluorescence microscopy GFP-FtsI localized to the division site during the later stages of cell growth and throughout septation. Localization of GFP-FtsI to the cell pole(s) was not observed unless the protein was overproduced about 10-fold. Membrane anchor alterations shown previously to impair division but not membrane insertion or transpeptidase activity were found to interfere with localization of GFP-FtsI to the division site. In contrast, GFP-FtsI localized well in the presence of β-lactam antibiotics that inhibit the transpeptidase activity of FtsI. Septal localization depended upon every other division protein tested (FtsZ, FtsA, FtsQ, and FtsL). We conclude that FtsI is a late recruit to the division site, and that its localization depends on an intact membrane anchor.
Details
- Title: Subtitle
- Localization of FtsI (PBP3) to the Septal Ring Requires Its Membrane Anchor, the Z Ring, FtsA, FtsQ, and FtsL
- Creators
- David S Weiss - Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115Joseph C Chen - Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115Jean-Marc Ghigo - Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115Dana Boyd - Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115Jon Beckwith - Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115
- Resource Type
- Journal article
- Publication Details
- Journal of bacteriology, Vol.181(2), pp.508-520
- Publisher
- American Society for Microbiology
- DOI
- 10.1128/jb.181.2.508-520.1999
- PMID
- 9882665
- PMCID
- PMC93405
- ISSN
- 0021-9193
- eISSN
- 1098-5530
- Language
- English
- Date published
- 01/1999
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984001116602771
Metrics
13 Record Views