PdhS, an old-pole-localized histidine kinase, recruits the fumarase FumC in Brucella abortus.
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.
Mignolet
Johann
J
Molecular Biology Research Unit (URBM), University of Namur (FUNDP), 61 rue de Bruxelles, B-5000 Namur, Belgium.
Van der Henst
Charles
C
Nicolas
Cécile
C
Deghelt
Michaël
M
Dotreppe
Delphine
D
Letesson
Jean-Jacques
JJ
De Bolle
Xavier
X
D002003:Brucella abortus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D005649:Fumarate Hydratase / Q000378:metabolism*; D017353:Gene Deletion; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology; D000071677:Histidine Kinase; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism*; D021381:Protein Transport
D011494:Protein Kinases; D000071677:Histidine Kinase; D005649:Fumarate Hydratase
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