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PAS Domains: Internal Sensors of Oxygen, Redox Potential, and Light
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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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“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.”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [59]
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Cites
1 retracted
Hypoxia-inducible Factor 1α (HIF-1α) Is a Non-heme Iron Protein
Srinivas, V., Zhu, X., Salceda, S., Nakamura, R., & Caro, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18019 · Cited by 69
RetractedBasic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
Kaneko, T., Sato, S., Kotani, H., Tanaka, A., Asamizu, E., Nakamura, Y., Miyajima, N., Hirosawa, M., Sugiura, M., Sasamoto, S., et al. (1996) · DNA Research · doi:10.1093/dnares/3.3.185 · Cited by 2,434
Sanguinetti, M. C., Jiang, C., Curran, M. E., & Keating, M. T. (1995) · Cell · doi:10.1016/0092-8674(95)90340-2 · Cited by 2,422
A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome
Curran, M. E., Splawski, I., Timothy, K. W., Vincent, G. M., Green, E. D., & Keating, M. T. (1995) · Cell · doi:10.1016/0092-8674(95)90358-5 · Cited by 2,253
Kaneko, T., Sato, S., Kotani, H., Tanaka, A., Asamizu, E., Nakamura, Y., Miyajima, N., Hirosawa, M., Sugiura, M., Sasamoto, S., et al. (1996) · DNA Research · doi:10.1093/dnares/3.3.109 · Cited by 2,132
Huang, L. E., Gu, J., Schau, M., & Bunn, H. F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.7987 · Cited by 2,113
Role of the CLOCK Protein in the Mammalian Circadian Mechanism
Gekakis, N., Staknis, D., Nguyen, H. B., Davis, F. C., Wilsbacher, L. D., King, D. P., Takahashi, J. S., & Weitz, C. J. (1998) · Science · doi:10.1126/science.280.5369.1564 · Cited by 2,035
SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins
Koch, C. A., Anderson, D. H., Moran, M. F., Ellis, C. A., & Pawson, T. J. (1991) · Science · doi:10.1126/science.1708916 · Cited by 1,868
Research works printed but not linked: 2
- 10.1016/S0022-2836(05)80360-2 · DOI · Paper page
- Lynch A. S. Lin E. C. C. Responses to molecular oxygen Escherichia coli and Salmonella: cellular and molecular biology 2nd ed. Neidhardt F. C. Curtiss R. III Ingraham J. L. Lin E. C. C. Low K. B. Magasanik B. Reznikoff W. S. Riley M. Schaechter M. Umbarger H. E. 1 1996 1526 1538 ASM Press Washington, D.C
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Denison, M. S., & Nagy, S. R. (2003) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.135828 · Cited by 1,895
HIF-1: mediator of physiological and pathophysiological responses to hypoxia
Semenza, G. L. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.4.1474 · Cited by 1,822
Overview of Structure and Function of Mammalian Cilia
Satir, P., & Christensen, S. T. (2007) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.040705.141236 · Cited by 1,142
Membrane fluidity and its roles in the perception of environmental signals
Los, D. A., & Murata, N. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.08.002 · Cited by 1,020
Phototropin Blue-Light Receptors
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Tanimoto, K., Makino, Y., Pereira, T., & Poellinger, L. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4298 · Cited by 928
Phototropins 1 and 2: versatile plant blue-light receptors
Briggs, W. R., & Christie, J. M. (2002) · Trends in Plant Science · doi:10.1016/s1360-1385(02)02245-8 · Cited by 785
Sakai, T., Kagawa, T., Kasahara, M., Swartz, T. E., Christie, J. M., Briggs, W. R., Wada, M., & Okada, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101137598 · Cited by 715
Aryl hydrocarbon receptors: diversity and evolution
Hahn, M. E. (2002) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00070-4 · Cited by 642
Molecular Mechanisms of Two-Component Signal Transduction
Zschiedrich, C. P., Keidel, V., & Szurmant, H. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.003 · Cited by 540
Scortegagna, M., Ding, K., Oktay, Y., Gaur, A., Thurmond, F., Yan, L.-J., Marck, B. T., Matsumoto, A. M., Shelton, J. M., Richardson, J. A., et al. (2003) · Nature Genetics · doi:10.1038/ng1266 · Cited by 496
Structure and function of plant photoreceptors
Möglich, A., Yang, X., Ayers, R. A., & Moffat, K. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112259 · Cited by 499
Ligand binding and activation of the Ah receptor
Denison, M. S., Pandini, A., Nagy, S. R., Baldwin, E. P., & Bonati, L. (2002) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00063-7 · Cited by 485
Cellular and Subcellular Localization of Phototropin 1
Sakamoto, K., & Briggs, W. R. (2002) · The Plant Cell · doi:10.1105/tpc.003293 · Cited by 405
Perspectives on Oxygen Sensing
Semenza, G. L. (1999) · Cell · doi:10.1016/s0092-8674(00)81957-1 · Cited by 385
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McIntosh, B. E., Hogenesch, J. B., & Bradfield, C. A. (2010) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021909-135922 · Cited by 352
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Erbel-Sieler, C., Dudley, C., Zhou, Y., Wu, X., Estill, S. J., Han, T., Diaz-Arrastia, R., Brunskill, E. W., Potter, S. S., & McKnight, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405310101 · Cited by 178
Casas-Flores, S., Rios-Momberg, M., Bibbins, M., Ponce-Noyola, P., & Herrera-Estrella, A. (2004) · Microbiology · doi:10.1099/mic.0.27346-0 · Cited by 172
Pandini, A., Denison, M. S., Song, Y., Soshilov, A. A., & Bonati, L. (2007) · Biochemistry · doi:10.1021/bi061460t · Cited by 160
Shoot phototropism in higher plants: New light through old concepts
Christie, J. M., & Murphy, A. S. (2013) · American Journal of Botany · doi:10.3732/ajb.1200340 · Cited by 152
Trends in protein evolution inferred from sequence and structure analysis
Aravind, L., Mazumder, R., Vasudevan, S., & Koonin, E. V. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00334-2 · Cited by 148
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Salomon, M., Lempert, U., & Rüdiger, W. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.06.081 · Cited by 116
In Vivo Phosphorylation Site Mapping and Functional Characterization of Arabidopsis Phototropin 1
Sullivan, S., Thomson, C. E., Lamont, D. J., Jones, M. A., & Christie, J. M. (2008) · Molecular Plant · doi:10.1093/mp/ssm017 · Cited by 107
Definition of a Dioxin Receptor Mutant That Is a Constitutive Activator of Transcription
McGuire, J., Okamoto, K., Whitelaw, M. L., Tanaka, H., & Poellinger, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105607200 · Cited by 102
Ambra, R., Grimaldi, B., Zamboni, S., Filetici, P., Macino, G., & Ballario, P. (2004) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2004.02.004 · Cited by 81
Bouchnak, I., & van Wijk, K. J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100338 · Cited by 77
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Neuronal PAS domain proteins 1 and 3 are master regulators of neuropsychiatric risk genes
Michaelson, J. J., Shin, M.-K., Koh, J.-Y., Brueggeman, L., Zhang, A., Katzman, A., McDaniel, L., Fang, M., Pufall, M., & Pieper, A. A. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.03.021 · Cited by 47
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Bhaya, D., Vaulot, D., Amin, P., Takahashi, A. W., & Grossman, A. R. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.20.5692-5699.2000 · Cited by 42
Loza‐Correa, M., Sahr, T., Rolando, M., Daniels, C., Petit, P., Skarina, T., Gomez Valero, L., Dervins‐Ravault, D., Honoré, N., Savchenko, A., et al. (2014) · Environmental Microbiology · doi:10.1111/1462-2920.12223 · Cited by 34
Kudo, K., Takeuchi, T., Murakami, Y., Ebina, M., & Kikuchi, H. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.06.003 · Cited by 25
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Stone, B. B., Esmon, C. A., & Liscum, E. (2005) · Current Topics in Developmental Biology · doi:10.1016/s0070-2153(05)66007-3 · Cited by 13
Metadata
- Authors
- Taylor, B. L., & Zhulin, I. B.
- Affiliations
- Loma Linda University (US)
- <!--label omitted: 1-->Department of Microbiology and Molecular Genetics1 and
- ORCID
- Zhulin, Igor B.
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 1999-06
- Volume
- 63
- Issue
- 2
- Pages
- 479-506
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- PMC
- PMC98974
- 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
- bronze
- doi.org
- 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 › Biochemistry › 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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