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

par Mignolet, Johann ;Van Der Henst, Charles;Nicolas, Cécile;Deghelt, Michaël;Dotreppe, Delphine;Letesson, Jean-Jacques;De Bolle, Xavier
Référence Journal of bacteriology, 192, 12, page (3235-3239)
Publication Publié, 2010-06

Article révisé par les pairs

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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. Copyright © 2010, American Society for Microbiology. All Rights Reserved.