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PdhS, an old-pole-localized histidine kinase, recruits the fumarase FumC in Brucella abortus.

ABSTRACT: The bacterial pathogen Brucella abortus was recently demonstrated to recruit the essential cytoplasmic histidine kinase PdhS to its old pole. Here, we report identification of the fumarase FumC as a specific partner for the N-terminal "sensing" domain of PdhS, using an ORFeome-based yeast two-hybrid screen. We observed that FumC and PdhS colocalize at the old pole of B. abortus, while the other fumarase FumA is not polarly localized. FumC is not required for PdhS localization, and polar FumC localization is not FumA dependent. FumC homologs are not polarly localized in Sinorhizobium meliloti and Caulobacter crescentus, suggesting that polar recruitment of FumC by PdhS is evolutionarily recent.

SUBMITTER: Mignolet J

PROVIDER: S-EPMC2901695 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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PdhS, an old-pole-localized histidine kinase, recruits the fumarase FumC in Brucella abortus.

Mignolet Johann J Van der Henst Charles C Nicolas Cécile C Deghelt Michaël M Dotreppe Delphine D Letesson Jean-Jacques JJ De Bolle Xavier X

Journal of bacteriology 20100409 12

The bacterial pathogen Brucella abortus was recently demonstrated to recruit the essential cytoplasmic histidine kinase PdhS to its old pole. Here, we report identification of the fumarase FumC as a specific partner for the N-terminal "sensing" domain of PdhS, using an ORFeome-based yeast two-hybrid screen. We observed that FumC and PdhS colocalize at the old pole of B. abortus, while the other fumarase FumA is not polarly localized. FumC is not required for PdhS localization, and polar FumC loc ...[more]

PMID: 20382762

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