An α/β Hydrolase and Associated Per-ARNT-Sim Domain Comprise a Bipartite Sensing Module Coupled with Diverse Output Domains
2011

Bipartite Sensor Module in Diverse Bacteria

publication Evidence: moderate

Author Information

Author(s): Nadezhdin Eugene V., Brody Margaret S., Price Chester W.

Primary Institution: Department of Microbiology, University of California Davis, Davis, California, United States of America

Hypothesis

The RsbQ α/β hydrolase and RsbP serine phosphatase form a signaling pair required to activate the general stress factor σB of Bacillus subtilis in response to energy limitation.

Conclusion

The study identifies a bipartite sensing module that regulates various output domains in response to energy stress in bacteria.

Supporting Evidence

  • The study found 45 homologues of RsbQ and RsbP-PAS in diverse bacteria.
  • Alanine substitutions at four residues conferred a null phenotype in Bacillus subtilis, indicating their functional importance.
  • RsbQ and the PAS domain appear to form a sensory module that conveys signals to various output domains.

Takeaway

This study shows how bacteria can sense energy levels and respond to stress using a special signaling system made of two proteins.

Methodology

The study used bioinformatic and genetic analysis to investigate the RsbQ-RsbP signaling pathway in Bacillus subtilis.

Limitations

The physiological cue that initiates signal transduction via the RsbQ-PAS module remains unknown.

Digital Object Identifier (DOI)

10.1371/journal.pone.0025418

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