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J Biol Chem. 2013 Oct 18;288(42):30473-84. doi: 10.1074/jbc.M113.489914. Epub 2013 Sep 6.

Characterization of the AtsR hybrid sensor kinase phosphorelay pathway and identification of its response regulator in Burkholderia cenocepacia.

Author information

1
From the Centre for Human Immunology, Department of Microbiology and Immunology, Schulich School of Medicine, University of Western Ontario, London, Ontario N6A 5C1, Canada and.

Abstract

AtsR is a membrane-bound hybrid sensor kinase of Burkholderia cenocepacia that negatively regulates quorum sensing and virulence factors such as biofilm production, type 6-secretion, and protease secretion. Here we elucidate the mechanism of AtsR phosphorelay by site-directed mutagenesis of predicted histidine and aspartic acid phosphoacceptor residues. We demonstrate by in vitro phosphorylation that histidine 245 and aspartic acid 536 are conserved sites of phosphorylation in AtsR, and we also identify the cytosolic response regulator AtsT (BCAM0381) as a key component of the AtsR phosphorelay pathway. Monitoring the function of AtsR and its derivatives in vivo by measuring extracellular protease activity and swarming motility confirmed the in vitro phosphorylation results. Together we find that the AtsR receiver domain plays a fine-tuning role in determining the levels of phosphotransfer from its sensor kinase domain to the AtsT response regulator.

KEYWORDS:

Bacterial Protein Kinases; Cystic Fibrosis; Histidine Kinases; Macrophages; Phosphorylation; Protease; Transcription Regulation; Virulence Factors

PMID:
24014026
PMCID:
PMC3798511
DOI:
10.1074/jbc.M113.489914
[Indexed for MEDLINE]
Free PMC Article
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