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

Verfasser / Beitragende:
[Matthieu Bergé, Sébastien Campagne, Johann Mignolet, Seamus Holden, Laurence Théraulaz, Suliana Manley, Frédéric H.-T. Allain, Patrick H. Viollier]
Ort, Verlag, Jahr:
2016
Enthalten in:
eLife, 5, p. e20640
Format:
Artikel (online)
ID: 528785389
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024 7 0 |a 10.3929/ethz-b-000124547  |2 doi 
024 7 0 |a 10.7554/eLife.20640  |2 doi 
035 |a (ETHRESEARCH)oai:www.research-collecti.ethz.ch:20.500.11850/124547 
245 0 0 |a Modularity and determinants of a (bi-)polarization control system from free-living and obligate intracellular bacteria  |h [Elektronische Daten]  |c [Matthieu Bergé, Sébastien Campagne, Johann Mignolet, Seamus Holden, Laurence Théraulaz, Suliana Manley, Frédéric H.-T. Allain, Patrick H. Viollier] 
506 |a Open access  |2 ethresearch 
520 3 |a 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. 
540 |a Creative Commons Attribution 4.0 International  |u http://creativecommons.org/licenses/by/4.0  |2 ethresearch 
700 1 |a Bergé  |D Matthieu  |e joint author 
700 1 |a Campagne  |D Sébastien  |e joint author 
700 1 |a Mignolet  |D Johann  |e joint author 
700 1 |a Holden  |D Seamus  |e joint author 
700 1 |a Théraulaz  |D Laurence  |e joint author 
700 1 |a Manley  |D Suliana  |e joint author 
700 1 |a Allain  |D Frédéric H.-T  |e joint author 
700 1 |a Viollier  |D Patrick H.  |e joint author 
773 0 |t eLife  |d Cambridge : eLife Sciences Publishing  |g 5, p. e20640 
856 4 0 |u http://hdl.handle.net/20.500.11850/124547  |q text/html  |z WWW-Backlink auf das Repository (Open access) 
908 |D 1  |a Journal Article  |2 ethresearch 
950 |B ETHRESEARCH  |P 856  |E 40  |u http://hdl.handle.net/20.500.11850/124547  |q text/html  |z WWW-Backlink auf das Repository (Open access) 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Bergé  |D Matthieu  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Campagne  |D Sébastien  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Mignolet  |D Johann  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Holden  |D Seamus  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Théraulaz  |D Laurence  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Manley  |D Suliana  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Allain  |D Frédéric H.-T  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Viollier  |D Patrick H.  |e joint author 
950 |B ETHRESEARCH  |P 773  |E 0-  |t eLife  |d Cambridge : eLife Sciences Publishing  |g 5, p. e20640 
898 |a BK010053  |b XK010053  |c XK010000 
949 |B ETHRESEARCH  |F ETHRESEARCH  |b ETHRESEARCH  |j Journal Article  |c Open access