Bacterial Birth Scar Proteins Mark Future Flagellum Assembly Site

@article{Huitema2006BacterialBS,
  title={Bacterial Birth Scar Proteins Mark Future Flagellum Assembly Site},
  author={Edgar Huitema and Sean Pritchard and David T Matteson and Sunish Kumar Radhakrishnan and Patrick H. Viollier},
  journal={Cell},
  year={2006},
  volume={124},
  pages={1025-1037}
}

Figures from this paper

A multimeric pole-organizing protein critical for chromosome attachment , division and protein localization in Caulobacter
TLDR
Evidence is provided that Caulobacter crescentus uses a multimeric pole-organizing factor (PopZ) that serves as a hub to concurrently achieve several polarizing functions and that localization of PopZ largely relies on PopZ multimerization in chromosome-free regions, consistent with a self-organized mechanism.
A multidomain hub anchors the chromosome segregation and chemotactic machinery to the bacterial pole.
TLDR
HubP (hub of the pole), a polar transmembrane protein conserved in all vibrios, is identified that anchors three ParA-like ATPases to the cell poles and, through them, controls polar localization of the chromosome origin, the chemotactic machinery, and the flagellum in Vibrio cholerae.
Analysis of HubP-dependent cell pole protein targeting in Vibrio cholerae uncovers novel motility regulators
TLDR
Comp comparative proteomics, genetic and imaging approaches are used to identify additional HubP partners and demonstrate that at least six more proteins are subject to HubP-dependent polar localization, revealing an ever more versatile role for the landmark cell pole organizer HubP and identifying novel mechanisms of motility regulation.
Caulobacter PopZ forms a polar subdomain dictating sequential changes in pole composition and function
TLDR
It is proposed that pole‐specific control of PopZ function co‐ordinates polar development and cell cycle progression by enabling independent assembly and tethering activities at the two cell poles.
Coiled-coil protein Scy is a key component of a multiprotein assembly controlling polarized growth in Streptomyces
TLDR
It is proposed that Scy is a molecular “assembler,” which, by sequestering DivIVA, promotes the establishment of new polarity centers for de novo tip formation during branching, as well as supporting polarized growth at existing hyphal tips.
The role of FlhF and HubP as polar landmark proteins in Shewanella putrefaciens CN‐32
TLDR
It is hypothesized that a group of HubP/FimV homologs, characterized by a rather conserved N‐terminal periplasmic section required for polar targeting and a highly variable acidic cytoplasmic part, primarily mediating recruitment of client proteins, serves as polar markers in various bacterial species with respect to different cellular functions.
A Localized Complex of Two Protein Oligomers Controls the Orientation of Cell Polarity
TLDR
This work recapitulate the tripartite assembly of a cell fate signaling complex that forms during the G1-S transition in Caulobacter and demonstrates that the ordered assembly of this microdomain occurs via the polymeric network protein PopZ directly recruiting the polarity factor SpmX, which then recruits the histidine kinase DivJ to the developing cell pole.
...
...

References

SHOWING 1-10 OF 56 REFERENCES
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.
Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins
TLDR
A protein is identified, PodJ, that provides the positional information for the polar localization of both PleC and CpaE, and stimulates the response signaled by a two-component system in Caulobacter.
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.
Cytokinesis in Bacteria
TLDR
Work on two diverse rod-shaped bacteria, Escherichia coli and Bacillus subtilis, has defined a set of about 10 conserved proteins that are important for cell division in a wide range of eubacteria, with the exception of at least one penicillin-binding protein, which catalyzes a key step in cell wall synthesis in the division septum.
Identification of a polar targeting determinant for Bacillus subtilis DivIVA
TLDR
It is demonstrated that polar targeting of DivIVAR18C is not essential during vegetative growth because the mutant can recognize the cell division site and influences the localization of MinD, and it is shown that DivIV AR18C can function during sporulation because it can support the Spo0J/Soj orientation of the chromosome.
A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant
TLDR
The sequential degradation of PodJ appears to involve regulated intramembrane proteolysis (Rip) by MmpA, and it is determined that mmpA and yaeL can complement each other in C. crescentus and E. coli, indicating functional conservation.
Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE
TLDR
It is demonstrated that the two proteins interact directly and that domain II and possibly domain I of SpoIIE are required for the interaction and suggested that this self‐interaction plays a role in assembly of Spo IIE into the division machinery.
FlbT Couples Flagellum Assembly to Gene Expression in Caulobacter crescentus
TLDR
It is demonstrated that mutations in flbT, aflagellar gene of unknown function, can restore flagellin protein synthesis and the expression of fljK::lacZ protein fusions in class III flageLLar mutants, suggesting that coupling of flagesllin gene expression to assembly has a critical influence on regulating cell cycle expression.
A lytic transglycosylase homologue, PleA, is required for the assembly of pili and the flagellum at the Caulobacter crescentus cell pole
TLDR
It is argued that PleA facilitates the assembly of envelope‐spanning structures at the cell pole and was found to be present only during a short interval in the cell cycle that coincides with theAssembly of the flagellum and the pilus secretion apparatus.
...
...