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Journal of Bacteriology, December 2004, p. 8370-8379, Vol. 186, No. 24
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.24.8370-8379.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Functional Analysis of the Cell Division Protein FtsW of Escherichia coli
Soumya Pastoret,1
Claudine Fraipont,1
Tanneke den Blaauwen,2
Benoît Wolf,1
Mirjam E. G. Aarsman,2
André Piette,1
Annick Thomas,3
Robert Brasseur,3 and
Martine Nguyen-Distèche1*
Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, Liège,1
Centre de Biophysique Moléculaire Numérique, Faculté Universitaire des Sciences Agronomiques, Gembloux, Belgium,3
Swammerdam Institute for Life Sciences, Amsterdam, The Netherlands2
Received 25 June 2004/
Accepted 9 September 2004
Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in peptidoglycan assembly during cell elongation, division, and sporulation. This essential cell division protein has 10 transmembrane segments (TMSs). It is a late recruit to the division site and is required for subsequent recruitment of penicillin-binding protein 3 (PBP3) catalyzing peptide cross-linking. The results allow identification of several domains of the protein with distinct functions. The localization of PBP3 to the septum was found to be dependent on the periplasmic loop located between TMSs 9 and 10. The E240-A249 amphiphilic peptide in the periplasmic loop between TMSs 7 and 8 appears to be a key element in the functioning of FtsW in the septal peptidoglycan assembly machineries. The intracellular loop (containing the R166-F178 amphiphilic peptide) between TMSs 4 and 5 and Gly 311 in TMS 8 are important components of the amino acid sequence-folding information.
* Corresponding author. Mailing address: Centre d'Ingénierie des Protéines, Institut de Chimie, Bât. allée de la Chimie, 3, B-4000 Liège, Belgium. Phone: (32) 4 3663397. Fax: (32) 4 3663364. E-mail:
mng.disteche{at}ulg.ac.be.
Supplemental material for this article may be found at http://jb.asm.org/.
Journal of Bacteriology, December 2004, p. 8370-8379, Vol. 186, No. 24
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.24.8370-8379.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
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