NDLI: Role of the PAS Sensor Domains in the Bacillus subtilis Sporulation Kinase KinA

Content Provider	PubMed Central
Author	Winnen, Brit Anderson, Eric Cole, James L. King, Glenn F. Rowland, Susan L.
Copyright Year	2013
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.
Related Links	http://dx.doi.org/10.1128/JB.00096-13
Starting Page	2349
File Format	PDF
ISSN	10985530
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	10
Volume Number	195
Language	English
Publisher	American Society for Microbiology
Publisher Date	2013-05-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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The Threshold Level of the Sensor Histidine Kinase KinA Governs Entry into Sporulation in Bacillus subtilis ▿ †

In Vivo Domain-Based Functional Analysis of the Major Sporulation Sensor Kinase, KinA, in Bacillus subtilis ▿ †

Isolation and characterization of kinC, a gene that encodes a sensor kinase homologous to the sporulation sensor kinases KinA and KinB in Bacillus subtilis.

Different roles for KinA, KinB, and KinC in the initiation of sporulation in Bacillus subtilis.

Expression of kinA and accumulation of sigma H at the onset of sporulation in Bacillus subtilis.

Sensor Domains Encoded in Bacillus anthracis Virulence Plasmids Prevent Sporulation by Hijacking a Sporulation Sensor Histidine Kinase

Expression of kinA and kinB of Bacillus subtilis, Necessary for Sporulation Initiation, Is under Positive Stringent Transcription Control

Bacillus subtilis early sporulation genes kinA, spo0F, and spo0A are transcribed by the RNA polymerase containing sigma H.

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Role of the PAS Sensor Domains in the Bacillus subtilis Sporulation Kinase KinA

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The Threshold Level of the Sensor Histidine Kinase KinA Governs Entry into Sporulation in Bacillus subtilis ▿ †

In Vivo Domain-Based Functional Analysis of the Major Sporulation Sensor Kinase, KinA, in Bacillus subtilis ▿ †

Isolation and characterization of kinC, a gene that encodes a sensor kinase homologous to the sporulation sensor kinases KinA and KinB in Bacillus subtilis.

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