A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
Open Access
- 7 May 2004
- journal article
- Published by Wiley in Molecular Microbiology
- Vol. 52 (5), 1315-1327
- https://doi.org/10.1111/j.1365-2958.2004.04044.x
Abstract
Summary Three membrane proteins required for cell division in Escherichia coli, FtsQ, FtsL and FtsB, localize to the cell septum. FtsL and FtsB, which each contain a leucine zipper-like sequence, are dependent on each other for this localization, and each of them is dependent on FtsQ. However, FtsQ is found at the cell division site in the absence of FtsL and FtsB. FtsQ, in turn, requires FtsK for its localization. Here, we show that FtsL, FtsB and FtsQ form a complex in vivo. Strikingly, this complex forms in the absence of FtsK, which is required for the localization of all three proteins to the mid-cell. These findings indicate that the FtsL, FtsB, FtsQ interactions can take place in cells before movement to the mid-cell and that migration to this position might occur only after the formation of the complex. Evidence indicating the regions of the three proteins involved in complex formation is presented. These findings provide the first example of preassembly of a subcomplex of cell division proteins before their localization to the septal region.Keywords
This publication has 42 references indexed in Scilit:
- Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiationMicrobiology, 2003
- The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin‐arginine transport pathwayMolecular Microbiology, 2003
- Cytokinesis in EukaryotesMicrobiology and Molecular Biology Reviews, 2002
- Analysis of ftsQ Mutant Alleles in Escherichia coli : Complementation, Septal Localization, and Recruitment of Downstream Cell Division ProteinsJournal of Bacteriology, 2002
- The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assemblyBiochemical Journal, 2001
- Septal Localization of the Membrane-Bound Division Proteins of Bacillus subtilis DivIB and DivIC Is Codependent Only at High Temperatures and Requires FtsZJournal of Bacteriology, 2000
- Lambda repressor N-terminal DNA-binding domain as an assay for protein transmembrane segment interactions in VivoJournal of Molecular Biology, 1998
- Characterization of the essential cell division gene ftsL (yllD ) of Bacillus subtilis and its role in the assembly of the division apparatusMolecular Microbiology, 1998
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970