Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA

Winnen, Brit, Anderson, Eric, Cole, James L., King, Glenn F. and Rowland, S. L. (2013) Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA. Journal of Bacteriology, 195 10: 2349-2358. doi:10.1128/JB.00096-13

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Author Winnen, Brit
Anderson, Eric
Cole, James L.
King, Glenn F.
Rowland, S. L.
Title Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA
Formatted title
Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1098-5530
1067-8832
Publication date 2013-05-01
Sub-type Article (original research)
DOI 10.1128/JB.00096-13
Open Access Status File (Publisher version)
Volume 195
Issue 10
Start page 2349
End page 2358
Total pages 10
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2014
Language eng
Formatted abstract
Histidine kinases are sophisticated molecular sensors that are used by bacteria to detect and respond to a multitude of environmental signals. KinA is the major histidine kinase required for initiation of sporulation upon nutrient deprivation in Bacillus subtilis. KinA has a large N-terminal region (residues 1 to 382) that is uniquely composed of three tandem Per-ARNT-Sim (PAS) domains that have been proposed to constitute a sensor module. To further enhance our understanding of this “sensor” region, we defined the boundaries that give rise to the minimal autonomously folded PAS domains and analyzed their homo- and heteroassociation properties using analytical ultracentrifugation, nuclear magnetic resonance (NMR) spectroscopy, and multiangle laser light scattering. We show that PASA self-associates very weakly, while PASC is primarily a monomer. In contrast, PASB forms a stable dimer (Kd [dissociation constant] of <10 nM), and it appears to be the main N-terminal determinant of KinA dimerization. Analysis of KinA mutants deficient for one or more PAS domains revealed a critical role for PASB, but not PASA, in autophosphorylation of KinA. Our findings suggest that dimerization of PASB is important for keeping the catalytic domain of KinA in a functional conformation. We use this information to propose a model for the structure of the N-terminal sensor module of KinA.
Keyword 2-component signal-transduction
Size-distribution analysis
Histidine kinase
Sedimentation-velocity
Analytical ultracentrifugation
Transcription factor
Ligand-binding
Governs entry
Phosphorelay
Initiation
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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Created: Wed, 17 Apr 2013, 13:30:01 EST by Susan Allen on behalf of Institute for Molecular Bioscience