PMID:20363951
| Citation |
Gonzalez, MD, Akbay, EA, Boyd, D and Beckwith, J (2010) Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. J. Bacteriol. 192:2757-68 |
|---|---|
| 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. |
| Links |
PubMed PMC2876486 Online version:10.1128/JB.01609-09 |
| Keywords |
Amino Acid Sequence; Blotting, Western; Cell Cycle Proteins/chemistry; Cell Cycle Proteins/classification; Cell Cycle Proteins/genetics; Cell Cycle Proteins/metabolism; Computational Biology; Electrophoresis, Polyacrylamide Gel; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/classification; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Immunoprecipitation; Membrane Proteins/chemistry; Membrane Proteins/classification; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Sequence Data; Phylogeny; Protein Binding; Protein Structure, Tertiary |
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