Cited by 1,632Hemoglobin structure and functionCircadian rhythm and melatoninRedox biology and oxidative stress

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

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Taylor, Barry L., Zhulin, Igor B.·1999·Microbiology and Molecular Biology Reviews

Abstract

SUMMARY: 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.

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Crossref · 10.1128/mmbr.63.2.479-506.1999

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269 of 269 references verified0 citation errors · 0 not checkable

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  • PAS domains show high structural conservation of α and β folds, including a five-stranded β-sheet and a long central helix (helical connector) generally linked to a bulge of three small helices.

    “Besides the high ductility in signal responses developed by the PAS domains (59), these show a high structural conservation of the α and β folds. This includes a five-stranded β -sheet and a long central helix (helical connector) generally linked to a bulge of three small helices.”

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Authors
Taylor, B. L., & Zhulin, I. B.
Affiliations
  • Loma Linda University (US)
  • <!--label omitted: 1-->Department of Microbiology and Molecular Genetics1 and
Venue
Microbiology and Molecular Biology Reviews
Published
1999-06
Volume
63
Issue
2
Pages
479-506
ISSN
  • 1092-2172 (ISSN-L)
  • 1098-5557
OpenAlex
W2122023734
Cited by
1,632
References
269
Citations by year
2026: 19 · 2025: 36 · 2024: 31 · 2023: 37 · 2022: 30 · 2021: 51 · 2020: 49 · 2019: 55 · 2018: 44 · 2017: 45 · 2016: 39 · 2015: 55 · 2014: 71 · 2013: 61 · 2012: 63
FWCI
5.55
Type
journal article
Language
en
Open access
Locations
  • Microbiology and Molecular Biology Reviews (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of General Medical Sciences (GM-29481, R01GM029481)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords
PAS domain, oxygen sensing, redox signaling, optical sensing, signal transduction, cofactors, electron transport, hypoxia-inducible factor, voltage-gated ion channels, circadian clock
MeSH terms
Amino Acid Sequence, Animals, DNA-Binding Proteins, Electron Transport, Eukaryotic Cells, Humans, Light, Molecular Sequence Data, Oxidation-Reduction, Oxygen, Prokaryotic Cells, Potassium Channels, Signal Transduction, Sequence Alignment, Helix-Loop-Helix Motifs, Bacterial Physiological Phenomena

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