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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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.

Original languageEnglish
Pages (from-to)3235-9
Number of pages5
JournalJ Bacteriol
Issue number12
Publication statusPublished - 2010



  • Brucella abortus
  • Fumarate Hydratase
  • Gene Deletion
  • Gene Expression Regulation, Bacterial
  • Histidine Kinase
  • Protein Binding
  • Protein Kinases
  • Protein Transport
  • Journal Article
  • Research Support, Non-U.S. Gov't

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