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

doi:10.1128/JB.00066-10

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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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.

Original language	English
Pages (from-to)	3235-9
Number of pages	5
Journal	Journal of Bacteriology
Volume	192
Issue number	12
DOIs	https://doi.org/10.1128/JB.00066-10
Publication status	Published - 2010

Keywords

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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10.1128/JB.00066-10

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J. Bacteriol.-2010-Mignolet-3235-9
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title = "PdhS, an old-pole-localized histidine kinase, recruits the fumarase FumC in Brucella abortus",

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.",

keywords = "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",

author = "Johann Mignolet and {Van der Henst}, Charles and C{\'e}cile Nicolas and Micha{\"e}l Deghelt and Delphine Dotreppe and Jean-Jacques Letesson and {De Bolle}, Xavier",

year = "2010",

doi = "10.1128/JB.00066-10",

language = "English",

volume = "192",

pages = "3235--9",

journal = "Journal of Bacteriology",

issn = "0021-9193",

publisher = "American Society for Microbiology",

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TY - JOUR

T1 - PdhS, an old-pole-localized histidine kinase, recruits the fumarase FumC in Brucella abortus

AU - Mignolet, Johann

AU - Van der Henst, Charles

AU - Nicolas, Cécile

AU - Deghelt, Michaël

AU - Dotreppe, Delphine

AU - Letesson, Jean-Jacques

AU - De Bolle, Xavier

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

KW - Brucella abortus

KW - Fumarate Hydratase

KW - Gene Deletion

KW - Gene Expression Regulation, Bacterial

KW - Histidine Kinase

KW - Protein Binding

KW - Protein Kinases

KW - Protein Transport

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1128/JB.00066-10

DO - 10.1128/JB.00066-10

M3 - Article

C2 - 20382762

SN - 0021-9193

VL - 192

SP - 3235

EP - 3239

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 12

ER -

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

Abstract

Keywords

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