Ontology highlight
ABSTRACT:
SUBMITTER: Berge M
PROVIDER: S-EPMC5182065 | biostudies-literature | 2016 Dec
REPOSITORIES: biostudies-literature
Bergé Matthieu M Campagne Sébastien S Mignolet Johann J Holden Seamus S Théraulaz Laurence L Manley Suliana S Allain Frédéric H-T FH Viollier Patrick H PH
eLife 20161223
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 <i>Caulobacter crescentus</i> and an orthologous system from an obligate intracellular (rickettsial) pathogen. The NMR solution structure of the zinc-finger (ZnR) domain from the bifuncti ...[more]