A multidomain hub anchors the chromosome segregation and chemotactic machinery to the bacterial pole.

@article{Yamaichi2012AMH,
  title={A multidomain hub anchors the chromosome segregation and chemotactic machinery to the bacterial pole.},
  author={Yoshiharu Yamaichi and Raphael J. Bruckner and Simon Ringgaard and Andrea M{\"o}ll and D. Ewen Cameron and Ariane Briegel and Grant J. Jensen and Brigid M. Davis and Matthew K. Waldor},
  journal={Genes \& development},
  year={2012},
  volume={26 20},
  pages={
          2348-60
        }
}
The cell poles constitute key subcellular domains that are often critical for motility, chemotaxis, and chromosome segregation in rod-shaped bacteria. However, in nearly all rods, the processes that underlie the formation, recognition, and perpetuation of the polar domains are largely unknown. Here, in Vibrio cholerae, we identified HubP (hub of the pole), a polar transmembrane protein conserved in all vibrios, that anchors three ParA-like ATPases to the cell poles and, through them, controls… 

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References

SHOWING 1-10 OF 47 REFERENCES
A family of ParA-like ATPases promotes cell pole maturation by facilitating polar localization of chemotaxis proteins.
TLDR
These findings indicate that ParC promotes the efficiency of chemotactic signaling processes, in particular, ParC-facilitated development of a functional chemotaxis apparatus at the new pole readies this site for its development into a functional old pole after cell division.
A dynamically localized histidine kinase controls the asymmetric distribution of polar pili proteins
TLDR
It is demonstrated that the PleC histidine kinase, a two‐component signal transduction protein shown previously to localize to the piliated cell pole before and during pilus assembly, controls the accumulation of the pilin subunit, PilA.
Negative membrane curvature as a cue for subcellular localization of a bacterial protein
TLDR
It is reported that localization of the peripheral membrane protein DivIVA is determined in whole or in part by recognition of negative membrane curvature and that regions of the protein near the N and C terminus are important for localization.
Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site.
TLDR
This work shows that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed, and recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles.
RodZ, a component of the bacterial core morphogenic apparatus
TLDR
A key missing player in the cytoskeleton-based growth machinery enabling heritable and defined cellular forms in bacteria is uncovers in Caulobacter crescentus and Escherichia coli.
...
...