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The protein network of bacterial motility.

Rajagopala SV, Titz B, Goll J, Parrish JR, Wohlbold K, McKevitt MT, Palzkill T, Mori H, Finley RL, Uetz P - Mol. Syst. Biol. (2007)

Bottom Line: Comparing our interaction data with motility phenotypes from E. coli, Bacillus subtilis, and Helicobacter pylori, we found 23 hitherto uncharacterized proteins involved in motility.Integration of phylogenetic information with our interaction and phenotyping data reveals a conserved core of motility proteins, which appear to have recruited many additional species-specific components over time.Our interaction data also predict 18,110 interactions for 64 flagellated bacteria.

View Article: PubMed Central - PubMed

Affiliation: Institute of Genetics, Forschungszentrum Karlsruhe, Karlsruhe, Germany.

ABSTRACT
Motility is achieved in most bacterial species by the flagellar apparatus. It consists of dozens of different proteins with thousands of individual subunits. The published literature about bacterial chemotaxis and flagella documented 51 protein-protein interactions (PPIs) so far. We have screened whole genome two-hybrid arrays of Treponema pallidum and Campylobacter jejuni for PPIs involving known flagellar proteins and recovered 176 and 140 high-confidence interactions involving 110 and 133 proteins, respectively. To explore the biological relevance of these interactions, we tested an Escherichia coli gene deletion array for motility defects (using swarming assays) and found 159 gene deletion strains to have reduced or no motility. Comparing our interaction data with motility phenotypes from E. coli, Bacillus subtilis, and Helicobacter pylori, we found 23 hitherto uncharacterized proteins involved in motility. Integration of phylogenetic information with our interaction and phenotyping data reveals a conserved core of motility proteins, which appear to have recruited many additional species-specific components over time. Our interaction data also predict 18,110 interactions for 64 flagellated bacteria.

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The motility protein interaction network of T. pallidum. Blue nodes are known motility proteins, whereas black proteins are proteins of yet unknown function. Proteins with a motility phenotype in either E. coli or B. subtilis or H. pylori are indicated as octagons. See legend for other functional assignments. The motility network of C. jejuni is shown in Supplementary Figure S2.
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f2: The motility protein interaction network of T. pallidum. Blue nodes are known motility proteins, whereas black proteins are proteins of yet unknown function. Proteins with a motility phenotype in either E. coli or B. subtilis or H. pylori are indicated as octagons. See legend for other functional assignments. The motility network of C. jejuni is shown in Supplementary Figure S2.

Mentions: Many features of the bacterial flagellum have changed over the course of evolution. This is reflected in the surprisingly different composition and protein interaction patterns in the flagella of different species, which may reflect adaptations to species-specific motility needs (compare Figure 2 and Supplementary Figure S2). While the overall conservation allows us to predict ∼18 000 interactions for 64 proteomes of flagellated bacteria, it remains to be seen how many of them are functional.


The protein network of bacterial motility.

Rajagopala SV, Titz B, Goll J, Parrish JR, Wohlbold K, McKevitt MT, Palzkill T, Mori H, Finley RL, Uetz P - Mol. Syst. Biol. (2007)

The motility protein interaction network of T. pallidum. Blue nodes are known motility proteins, whereas black proteins are proteins of yet unknown function. Proteins with a motility phenotype in either E. coli or B. subtilis or H. pylori are indicated as octagons. See legend for other functional assignments. The motility network of C. jejuni is shown in Supplementary Figure S2.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC1943423&req=5

f2: The motility protein interaction network of T. pallidum. Blue nodes are known motility proteins, whereas black proteins are proteins of yet unknown function. Proteins with a motility phenotype in either E. coli or B. subtilis or H. pylori are indicated as octagons. See legend for other functional assignments. The motility network of C. jejuni is shown in Supplementary Figure S2.
Mentions: Many features of the bacterial flagellum have changed over the course of evolution. This is reflected in the surprisingly different composition and protein interaction patterns in the flagella of different species, which may reflect adaptations to species-specific motility needs (compare Figure 2 and Supplementary Figure S2). While the overall conservation allows us to predict ∼18 000 interactions for 64 proteomes of flagellated bacteria, it remains to be seen how many of them are functional.

Bottom Line: Comparing our interaction data with motility phenotypes from E. coli, Bacillus subtilis, and Helicobacter pylori, we found 23 hitherto uncharacterized proteins involved in motility.Integration of phylogenetic information with our interaction and phenotyping data reveals a conserved core of motility proteins, which appear to have recruited many additional species-specific components over time.Our interaction data also predict 18,110 interactions for 64 flagellated bacteria.

View Article: PubMed Central - PubMed

Affiliation: Institute of Genetics, Forschungszentrum Karlsruhe, Karlsruhe, Germany.

ABSTRACT
Motility is achieved in most bacterial species by the flagellar apparatus. It consists of dozens of different proteins with thousands of individual subunits. The published literature about bacterial chemotaxis and flagella documented 51 protein-protein interactions (PPIs) so far. We have screened whole genome two-hybrid arrays of Treponema pallidum and Campylobacter jejuni for PPIs involving known flagellar proteins and recovered 176 and 140 high-confidence interactions involving 110 and 133 proteins, respectively. To explore the biological relevance of these interactions, we tested an Escherichia coli gene deletion array for motility defects (using swarming assays) and found 159 gene deletion strains to have reduced or no motility. Comparing our interaction data with motility phenotypes from E. coli, Bacillus subtilis, and Helicobacter pylori, we found 23 hitherto uncharacterized proteins involved in motility. Integration of phylogenetic information with our interaction and phenotyping data reveals a conserved core of motility proteins, which appear to have recruited many additional species-specific components over time. Our interaction data also predict 18,110 interactions for 64 flagellated bacteria.

Show MeSH
Related in: MedlinePlus