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Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex.
- Source :
-
Journal of bacteriology [J Bacteriol] 2010 Jun; Vol. 192 (11), pp. 2757-68. Date of Electronic Publication: 2010 Apr 02. - Publication Year :
- 2010
-
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.
- Subjects :
- Amino Acid Sequence
Blotting, Western
Cell Cycle Proteins chemistry
Cell Cycle Proteins classification
Cell Cycle Proteins genetics
Computational Biology
Electrophoresis, Polyacrylamide Gel
Escherichia coli Proteins chemistry
Escherichia coli Proteins classification
Escherichia coli Proteins genetics
Immunoprecipitation
Membrane Proteins chemistry
Membrane Proteins classification
Membrane Proteins genetics
Molecular Sequence Data
Phylogeny
Protein Binding
Protein Structure, Tertiary
Cell Cycle Proteins metabolism
Escherichia coli Proteins metabolism
Membrane Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1098-5530
- Volume :
- 192
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Journal of bacteriology
- Publication Type :
- Academic Journal
- Accession number :
- 20363951
- Full Text :
- https://doi.org/10.1128/JB.01609-09