1. PdhS, an Old-Pole-Localized Histidine Kinase, Recruits the Fumarase FumC in Brucella abortus
- Author
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Johann Mignolet, Delphine Dotreppe, Xavier De Bolle, Charles Van der Henst, Michaël Deghelt, Jean-Jacques Letesson, Cécile Nicolas, and Department of Bio-engineering Sciences
- Subjects
Histidine Kinase ,Brucella abortus ,Research Support ,Microbiology ,Fumarate Hydratase ,Microbial Cell Biology ,Journal Article ,Non-U.S. Gov't ,ORFeome ,Molecular Biology ,Histidine ,Sinorhizobium meliloti ,biology ,Caulobacter crescentus ,Histidine kinase ,Bacterial ,Gene Expression Regulation, Bacterial ,biology.organism_classification ,Transport protein ,Cell biology ,Protein Transport ,Gene Expression Regulation ,Cytoplasm ,Fumarase ,Protein Kinases ,Gene Deletion ,Protein Binding - 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.
- Published
- 2010