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

Johann Mignolet, Charles Van der Henst, Cécile Nicolas, Michaël Deghelt, Delphine Dotreppe, Jean-Jacques Letesson, Xavier De Bolle

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Résumé

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.

langue originaleAnglais
Pages (de - à)3235-9
Nombre de pages5
journalJ Bacteriol
Volume192
Numéro de publication12
Les DOIs
Etat de la publicationPublié - 2010

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