Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex

Mark D. Gonzalez, Esra A. Akbay, Dana Boyd, Jon Beckwith

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

A bioinformatic analysis of nearly 400 genomes indicates that the overwhelming majority of bacteria possess homologs of the Escherichia coli proteins FtsL, FtsB, and FtsQ, three proteins essential for cell division in that bacterium. These three bitopic membrane proteins form a subcomplex in vivo, independent of the other cell division proteins. Here we analyze the domains of E. coli FtsL that are involved in the interaction with other cell division proteins and important for the assembly of the divisome. We show that FtsL, as we have found previously with FtsB, packs an enormous amount of information in its sequence for interactions with proteins upstream and downstream in the assembly pathway. Given their size, it is likely that the sole function of the complex of these two proteins is to act as a scaffold for divisome assembly.

Original languageEnglish (US)
Pages (from-to)2757-2768
Number of pages12
JournalJournal of Bacteriology
Volume192
Issue number11
DOIs
StatePublished - Jun 1 2010

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Cell Division
Proteins
Bacteria
Escherichia coli Proteins
Computational Biology
Membrane Proteins
Genome
Escherichia coli

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. / Gonzalez, Mark D.; Akbay, Esra A.; Boyd, Dana; Beckwith, Jon.

In: Journal of Bacteriology, Vol. 192, No. 11, 01.06.2010, p. 2757-2768.

Research output: Contribution to journalArticle

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