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

TitlePdhS, an old-pole-localized histidine kinase, recruits the fumarase FumC in Brucella abortus.
Publication TypeJournal Article
Year of Publication2010
AuthorsMignolet, J., C. Van der Henst, C. Nicolas, M. Deghelt, D. Dotreppe, J-J. Letesson, and X. De Bolle
JournalJ Bacteriol
Volume192
Issue12
Pagination3235-9
Date Published2010 Jun
ISSN1098-5530
KeywordsBrucella abortus, Fumarate Hydratase, Gene Deletion, Gene Expression Regulation, Bacterial, Histidine Kinase, Protein Binding, Protein Kinases, Protein Transport
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.

DOI10.1128/JB.00066-10
Alternate JournalJ. Bacteriol.
PubMed ID20382762
PubMed Central IDPMC2901695
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