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Journal of Bacteriology, October 2007, p. 7273-7280, Vol. 189, No. 20
0021-9193/07/$08.00+0 doi:10.1128/JB.00723-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Gert Jan Haan,1,
Tanneke den Blaauwen,3
Gregory Koningstein,1
Edwin van Bloois,1
Jon Beckwith,2 and
Joen Luirink1*
Molecular Microbiology, Institute for Molecular Cell Biology, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands,1 Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115,2 Swammerdam Institute for Life Sciences, Molecular Cytology, Kruislaan 316, 1098 SM Amsterdam, The Netherlands3
Received 8 May 2007/ Accepted 3 August 2007
The Escherichia coli cell division protein FtsQ is a central component of the divisome. FtsQ is a bitopic membrane protein with a large C-terminal periplasmic domain. In this work we investigated the role of the transmembrane segment (TMS) that anchors FtsQ in the cytoplasmic membrane. A set of TMS mutants was made and analyzed for the ability to complement an ftsQ mutant. Study of the various steps involved in FtsQ biogenesis revealed that one mutant (L29/32R;V38P) failed to functionally insert into the membrane, whereas another mutant (L29/32R) was correctly assembled and interacted with FtsB and FtsL but failed to localize efficiently to the cell division site. Our results indicate that the FtsQ TMS plays a role in FtsQ localization to the division site.
Published ahead of print on 10 August 2007.
Present address: Unité de Biochimie des Interactions Macromoléculaires, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France.
Present address: Centocor B.V., Einsteinweg 92, 2333 CD Leiden, The Netherlands.
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