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Microbiology and Molecular Biology Reviews, June 1999, p. 479-506, Vol. 63, No. 2
1092-2172/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

PAS Domains: Internal Sensors of Oxygen, Redox Potential, and Light

Barry L. Taylor1,2,* and Igor B. Zhulin1

Department of Microbiology and Molecular Genetics1 and Center for Molecular Biology and Gene Therapy,2 School of Medicine, Loma Linda University, Loma Linda, California 92350

PAS domains are newly recognized signaling domains that are widely distributed in proteins from members of the Archaea and Bacteria and from fungi, plants, insects, and vertebrates. They function as input modules in proteins that sense oxygen, redox potential, light, and some other stimuli. Specificity in sensing arises, in part, from different cofactors that may be associated with the PAS fold. Transduction of redox signals may be a common mechanistic theme in many different PAS domains. PAS proteins are always located intracellularly but may monitor the external as well as the internal environment. One way in which prokaryotic PAS proteins sense the environment is by detecting changes in the electron transport system. This serves as an early warning system for any reduction in cellular energy levels. Human PAS proteins include hypoxia-inducible factors and voltage-sensitive ion channels; other PAS proteins are integral components of circadian clocks. Although PAS domains were only recently identified, the signaling functions with which they are associated have long been recognized as fundamental properties of living cells.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA 92350. Phone: (909) 558-4480. Fax: (909) 558-4035. E-mail: blTaylor{at}som.llu.edu.

Microbiology and Molecular Biology Reviews, June 1999, p. 479-506, Vol. 63, No. 2
1092-2172/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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