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

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

Author information

1
Department Microbiology and Molecular Medicine, Institute of Genetics and Genomics in Geneva, Faculty of Medicine, University of Geneva, Geneva, Switzerland.
2
Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zürich, Zürich, Switzerland.
3
Laboratory of Experimental Biophysics, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.

Abstract

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

PMID:
28008852
PMCID:
PMC5182065
DOI:
10.7554/eLife.20640
[Indexed for MEDLINE]
Free PMC Article

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