In:
eLife, eLife Sciences Publications, Ltd, Vol. 5 ( 2016-12-23)
Kurzfassung:
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.
Materialart:
Online-Ressource
ISSN:
2050-084X
DOI:
10.7554/eLife.20640.001
DOI:
10.7554/eLife.20640.002
DOI:
10.7554/eLife.20640.003
DOI:
10.7554/eLife.20640.004
DOI:
10.7554/eLife.20640.005
DOI:
10.7554/eLife.20640.006
DOI:
10.7554/eLife.20640.007
DOI:
10.7554/eLife.20640.008
DOI:
10.7554/eLife.20640.009
DOI:
10.7554/eLife.20640.010
DOI:
10.7554/eLife.20640.011
DOI:
10.7554/eLife.20640.012
DOI:
10.7554/eLife.20640.013
DOI:
10.7554/eLife.20640.014
DOI:
10.7554/eLife.20640.015
DOI:
10.7554/eLife.20640.016
DOI:
10.7554/eLife.20640.017
DOI:
10.7554/eLife.20640.021
DOI:
10.7554/eLife.20640.022
DOI:
10.7554/eLife.20640.018
Sprache:
Englisch
Verlag:
eLife Sciences Publications, Ltd
Publikationsdatum:
2016
ZDB Id:
2687154-3
