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Journal of Bacteriology, January 1999, p. 508-520, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Localization of FtsI (PBP3) to the Septal Ring Requires Its Membrane Anchor, the Z Ring, FtsA, FtsQ, and FtsL

David S. Weiss,* Joseph C. Chen, Jean-Marc Ghigo,dagger Dana Boyd, and Jon Beckwith

Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115

Received 3 August 1998/Accepted 4 November 1998

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 beta -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.

* Corresponding author. Present address: Department of Microbiology, University of Iowa, 3403 Bowen Science Building, Iowa City, IA 52242. Phone: (319) 335-7785. Fax: (319) 335-7949. E-mail: david-weiss{at}uiowa.edu.

dagger Present address: Unité de Physiologie Cellulaire Institut Pasteur (CNRS URA 1300), 75724 Paris Cedex 15, France.

Journal of Bacteriology, January 1999, p. 508-520, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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