Modularity and determinants of a (bi-)polarization control system from free-living and obligate intracellular bacteria

Elife. 2016 Dec 23;5:e20640. doi: 10.7554/eLife.20640.


Although free-living and obligate intracellular bacteria are both polarized it is unclear whether the underlying polarization mechanisms and effector proteins are conserved. Here we dissect at the cytological, functional and structural level a conserved polarization module from the free living α-proteobacterium Caulobacter crescentus and an orthologous system from an obligate intracellular (rickettsial) pathogen. The NMR solution structure of the zinc-finger (ZnR) domain from the bifunctional and bipolar ZitP pilus assembly/motility regulator revealed conserved interaction determinants for PopZ, a bipolar matrix protein that anchors the ParB centromere-binding protein and other regulatory factors at the poles. We show that ZitP regulates cytokinesis and the localization of ParB and PopZ, targeting PopZ independently of the previously known binding sites for its client proteins. Through heterologous localization assays with rickettsial ZitP and PopZ orthologs, we document the shared ancestries, activities and structural determinants of a (bi-)polarization system encoded in free-living and obligate intracellular α-proteobacteria.

Keywords: Caulobacter crescentus; E. coli; PopZ; Rhodobacter sphaeroides; Rickettsia massiliae; ZitP; cell biology; chromosomes; genes; polarity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / metabolism*
  • Bacterial Proteins / metabolism*
  • Cation Transport Proteins / metabolism*
  • Caulobacter crescentus / enzymology*
  • Caulobacter crescentus / physiology
  • Cell Polarity
  • Cytokinesis*
  • Protein Binding
  • Protein Multimerization
  • Protein Transport
  • Rickettsia / enzymology*
  • Rickettsia / physiology


  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Cation Transport Proteins

Grants and funding

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.