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Journal of Bacteriology, January 2000, p. 116-129, Vol. 182, No. 1
Unité des Membranes Bactériennes,
Institut Pasteur (CNRS URA 1300), 75724 Paris Cedex 15, France,1 and Department of Microbiology
and Molecular Genetics, Harvard Medical School, Boston,
Massachusetts 021152
Received 1 July 1999/Accepted 11 October 1999
In Escherichia coli, nine essential cell division
proteins are known to localize to the division septum. FtsL is a 13-kDa bitopic membrane protein with a short cytoplasmic N-terminal domain, a
membrane-spanning segment, and a periplasmic domain that has a
repeated heptad motif characteristic of leucine zippers. Here, we
identify the requirements for FtsL septal localization and function. We
used green fluorescent protein fusions to FtsL proteins where domains
of FtsL had been exchanged with analogous domains from either its
Haemophilus influenzae homologue or the unrelated MalF
protein to show that both the membrane-spanning segment and the
periplasmic domain of FtsL are required for localization to the
division site. Mutagenesis of the periplasmic heptad repeat motif severely impaired both localization and function as well as the
ability of FtsL to drive the formation of sodium dodecyl sulfate-resistant multimers in vitro. These results are consistent with
the predicted propensity of the FtsL periplasmic domain to adopt a
coiled-coiled structure. This coiled-coil motif is conserved in all
gram-negative and gram-positive FtsL homologues identified so far. Our
data suggest that most of the FtsL molecule is a helical coiled coil
involved in FtsL multimerization.
0021-9193/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Cell Division in Escherichia coli: Role
of FtsL Domains in Septal Localization, Function, and
Oligomerization
*
Corresponding author. Mailing address: Unité des
Membranes Bactériennes, Institut Pasteur (CNRS URA 1300), 25 rue
du Dr. Roux, 75724 Paris Cedex 15, France. Phone: 33 (01) 45 68 88 14. Fax: 33 (01) 45 68 87 90. E-mail: jmghigo{at}pasteur.fr.
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