Oxygen sensing in yeast: Evidence for the involvement of the respiratory chain in regulating the transcription of a subset of hypoxic genes
Open accessAbstract
Oxygen availability affects the transcription of a number of genes in nearly all organisms. Although the molecular mechanisms for sensing oxygen are not precisely known, heme is thought to play a pivotal role. Here, we address the possibility that oxygen sensing in yeast, as in mammals, involves a redox-sensitive hemoprotein. We have found that carbon monoxide (CO) completely blocks the anoxia-induced expression of two hypoxic genes, OLE1 and CYC7, partially blocks the induction of a third gene, COX5b, and has no effect on the expression of other hypoxic or aerobic genes. In addition, transition metals (Co and Ni) induce the expression of OLE1 and CYC7 in a concentration-dependent manner under aerobic conditions. These findings suggest that the redox state of an oxygen-binding hemoprotein is involved in controlling the expression of at least two hypoxic yeast genes. By using mutants deficient in each of the two major yeast CO-binding hemoproteins (cytochrome c oxidase and flavohemoglobin), respiratory inhibitors, and cob1 and rho0 mutants, we have found that the respiratory chain is involved in the anoxic induction of these two genes and that cytochrome c oxidase is likely the hemoprotein "sensor." Our findings also indicate that there are at least two classes of hypoxic genes in yeast (CO sensitive and CO insensitive) and imply that multiple pathways/mechanisms are involved in modulating the expression of hypoxic yeast genes.
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A decrease in oxygen bioavailability causes a drop in heme and ergosterol levels that triggers the activation of signaling pathways that induce the expression of both hypoxic and ERG genes.
“Conversely, a decrease in oxygen bioavailability causes a drop in heme and ergosterol levels that triggers the activation of signaling pathways that induce the expression of both hypoxic and ERG genes [94].”
From Regulation of Ergosterol Biosynthesis in Saccharomyces cerevisiae (2020) · cites this paper as [94]
Several genome-wide expression studies under low oxygen conditions have reflected that the pattern of expression differs among ERG genes, although some general trends can be extracted.
“Several genome-wide expression studies based on microarray and RNA-Seq analyses under low oxygen conditions have reflected that the pattern of expression differs among ERG genes, although some general trends can be extracted [94,96,98,100,101,102,103].”
From Regulation of Ergosterol Biosynthesis in Saccharomyces cerevisiae (2020) · cites this paper as [94]
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Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589 · see citing works
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684 · see citing works
Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212 · see citing works
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167 · see citing works
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715 · see citing works
Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926 · see citing works
General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia.
Wang, G. L., & Semenza, G. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.4304 · Cited by 1,468 · see citing works
Oxygen sensing and molecular adaptation to hypoxia
Bunn, H. F., & Poyton, R. Ο. (1996) · Physiological Reviews · doi:10.1152/physrev.1996.76.3.839 · Cited by 1,185 · see citing works
Self-citationHochachka, P. W., Buck, L. T., Doll, C. J., & Land, S. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9493 · Cited by 1,105 · see citing works
Regulation of the Erythropoietin Gene: Evidence That the Oxygen Sensor Is a Heme Protein
Goldberg, M. A., Dunning, S. P., & Bunn, H. F. (1988) · Science · doi:10.1126/science.2849206 · Cited by 1,032 · see citing works
Intracellular Signaling by Reactive Oxygen Species during Hypoxia in Cardiomyocytes
Duranteau, J., Chandel, N. S., Kulisz, A., Shao, Z., & Schumacker, P. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11619 · Cited by 679 · see citing works
Goldberg, M. A., & Schneider, T. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41787-x · Cited by 582 · see citing works
CROSSTALK BETWEEN NUCLEAR AND MITOCHONDRIAL GENOMES
Poyton, R. Ο., & McEwen, J. E. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.003023 · Cited by 499 · see citing works
Self-citationMitochondrial Production of Superoxide Radical and Hydrogen Peroxide
Boveris, A. (1977) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-9035-4_5 · Cited by 427 · see citing works
Regulation of gene expression by oxygen in Saccharomyces cerevisiae
Zitomer, R. S., & Lowry, C. V. (1992) · Microbiological Reviews · doi:10.1128/mr.56.1.1-11.1992 · Cited by 413 · see citing works
Maxwell, P. H., Pugh, C. W., & Ratcliffe, P. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.6.2423 · Cited by 411 · see citing works
Elder, R. T., Loh, E. Y., & Davis, R. W. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.9.2432 · Cited by 410 · see citing works
Wilson, D. F., Rumsey, W. L., Green, T. J., & Vanderkooi, J. M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69126-4 · Cited by 387 · see citing works
Oxygen Sensing, Hypoxia-Inducible Factor-1 and the Regulation of Mammalian Gene Expression
Ratcliffe, P. J., O’rourke, J. F., Maxwell, P. H., & Pugh, C. W. (1998) · Journal of Experimental Biology · doi:10.1242/jeb.201.8.1153 · Cited by 367 · see citing works
Control of mitochondrial and cellular respiration by oxygen
Gnaiger, E., Steinlechner-Maran, R., Méndez, G., Eberl, T., & Margreiter, R. (1995) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf02111656 · Cited by 316 · see citing works
Heme binds to a short sequence that serves a regulatory function in diverse proteins.
Zhang, L., & Guarente, L. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07005.x · Cited by 290 · see citing works
Oxygen Sensing and the Transcriptional Regulation of Oxygen-Responsive Genes in Yeast
Kwast, K. E., Burke, P. V., & Poyton, R. Ο. (1998) · Journal of Experimental Biology · doi:10.1242/jeb.201.8.1177 · Cited by 249 · see citing works
Self-citationStudies on Cobalt Myoglobins and Hemoglobins
Yonetani, T., Yamamoto, H., & Woodrow, G. V. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42984-0 · Cited by 216 · see citing works
Rumsey, W. L., Schlosser, C., Nuutinen, E. M., Robiolio, M., & Wilson, D. F. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55409-0 · Cited by 211 · see citing works
Involvement of an NAD(P)H oxidase as a pO2 sensor protein in the rat carotid body
Cross, A. R., HENDERSON, L. M., Jones, O. T. G., Delpiano, M. A., Hentschel, J., & Acker, H. (1990) · Biochemical Journal · doi:10.1042/bj2720743 · Cited by 201 · see citing works
Cellular Respiration during Hypoxia
Chandel, N. S., Budinger, G. R. S., Choe, S. H., & Schumacker, P. T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18808 · Cited by 189 · see citing works
Erythropoietin: a Model System for Studying Oxygen-Dependent Gene Regulation
Bunn, H. F., Gu, J., Huang, L. E., Park, J., & Zhu, H. (1998) · Journal of Experimental Biology · doi:10.1242/jeb.201.8.1197 · Cited by 187 · see citing works
Tzagoloff, A., Akai, A., Needleman, R. B., et al. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40841-7 · Cited by 157 · see citing works
Choi, J., Stukey, J., Hwang, S., & Martin, C. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.7.3581 · Cited by 155 · see citing works
Hibernation during Hypoxia in Cardiomyocytes
Budinger, G. R. S., Duranteau, J., Chandel, N. S., & Schumacker, P. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3320 · Cited by 153 · see citing works
Carotid body O2 chemoreception and mitochondrial oxidative phosphorylation
Mulligan, E. M., Lahiri, S., & Storey, B. T. (1981) · Journal of Applied Physiology · doi:10.1152/jappl.1981.51.2.438 · Cited by 150 · see citing works
Molecular Oxygen Modulates Cytochrome c Oxidase Function
Chandel, N. S., Budinger, G. R. S., & Schumacker, P. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18672 · Cited by 139 · see citing works
Yeast flavohemoglobin is an ancient protein related to globins and a reductase family.
Zhu, H., & Riggs, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.11.5015 · Cited by 137 · see citing works
Ho, V. T., & Bunn, H. F. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0865 · Cited by 134 · see citing works
Burke, P. V., Raitt, D. C., Allen, L. A., Kellogg, E. A., & Poyton, R. Ο. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.23.14705 · Cited by 134 · see citing works
Self-citationWilson, D. F., Mokashi, A., Chugh, D. K., Vinogradov, S. A., Osanai, S., & Lahiri, S. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00887-6 · Cited by 122 · see citing works
The role of protein degradation in mitochondrial function and biogenesis
Rep, M., & Grivell, L. A. (1996) · Current Genetics · doi:10.1007/s002940050145 · Cited by 111 · see citing works
Two nonidentical forms of subunit V are functional in yeast cytochrome c oxidase.
Cumsky, M. G., Ko, C., Trueblood, C. E., et al. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.8.2235 · Cited by 105 · see citing works
Global Regulation of Mitochondrial Biogenesis in Saccharomyces cerevisiae
WINDE, J. H. D., & Grivell, L. A. (1993) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)61018-1 · Cited by 99 · see citing works
Kinetic trapping of oxygen in cell respiration
Verkhovsky, M. I., Morgan, J. E., Puustinen, A., & Wikström, M. K. F. (1996) · Nature · doi:10.1038/380268a0 · Cited by 98 · see citing works
Structure/Function Of Oxygen-Regulated Isoforms In Cytochrome c Oxidase
Burke, P. V., & Poyton, R. Ο. (1998) · Journal of Experimental Biology · doi:10.1242/jeb.201.8.1163 · Cited by 94 · see citing works
Self-citationFunction and Expression of Flavohemoglobin in Saccharomyces cerevisiae
Zhao, X.-J., Raitt, D. C., Burke, P. V., Clewell, A. S., Kwast, K. E., & Poyton, R. Ο. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.41.25131 · Cited by 93 · see citing works
Self-citationAllen, L. A., Zhao, X.-J., Caughey, W. S., & Poyton, R. Ο. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.1.110 · Cited by 93 · see citing works
Self-citationPhotometric characteristics of haem proteins in erythropoietin-producing hepatoma cells (HepG2)
Görlach, A., Holtermann, G., JELKMANN, W. E. B., et al. (1993) · Biochemical Journal · doi:10.1042/bj2900771 · Cited by 92 · see citing works
Waterland, R. A., Basu, A., Chance, B., & Poyton, R. Ο. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64304-6 · Cited by 90 · see citing works
Self-citationTSANG, S., Yin, X.-R., Guzzo-Arkuran, C., et al. (1993) · PubMed · Cited by 82 · see citing works
Sinclair, P., Gibbs, A. H., Sinclair, J. F., et al. (1979) · Biochemical Journal · doi:10.1042/bj1780529 · Cited by 70 · see citing works
Trueblood, C. E., & Poyton, R. Ο. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.10.3520-3526.1987 · Cited by 70 · see citing works
Self-citationReivich, M., Coburn, R. F., Lahiri, S., & Chance, B. (1977) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-9035-4 · Cited by 64 · see citing works
Properties of chemically modified Ni(II)Fe(II) hybrid hemoglobins
Shibayama, N., Morimoto, H., & Kitagawa, T. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90368-2 · Cited by 58 · see citing works
Kietzmann, T., Schmidt, H. E., Unthan-Fechner, K., et al. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2115 · Cited by 57 · see citing works
The Biogenesis of Yeast Mitochondria
Linnane, A. W., & HASLAM, J. M. (1970) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152802-7.50010-4 · Cited by 56 · see citing works
Mechanisms of O2 Sensing in the Carotid Body in Comparison With Other O2-Sensing Cells
Acker, H., & Xue, D. (1995) · Physiology · doi:10.1152/physiologyonline.1995.10.5.211 · Cited by 55 · see citing works
Regulation of Saccharomyces cerevisiae Flavohemoglobin Gene Expression
Crawford, M. J., Sherman, D. R., & Goldberg, D. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.12.6991 · Cited by 53 · see citing works
Acker, H. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb55698.x · Cited by 53 · see citing works
Lahiri, S., Buerk, D. G., Chugh, D. K., et al. (1995) · Brain Research · doi:10.1016/0006-8993(95)00420-u · Cited by 41 · see citing works
Obeso, A., Almaraz, L., & González, C. (1985) · Brain Research · doi:10.1016/0006-8993(85)90360-9 · Cited by 40 · see citing works
Chromophores in O2 Chemoreception: The Carotid Body Model
Lahiri, S. (1994) · Physiology · doi:10.1152/physiologyonline.1994.9.4.161 · Cited by 38 · see citing works
Oxygen regulated transcription of cytochrome and cytochrome oxidase genes in yeast
Poyton, R. Ο., & BURKE, P. (1992) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(05)80033-7 · Cited by 34 · see citing works
Self-citationTrueblood, C. E., & Poyton, R. Ο. (1988) · Genetics · doi:10.1093/genetics/120.3.671 · Cited by 31 · see citing works
Self-citationFormation of cobalt protoporphyrin by chicken hepatocytes in culture
Sinclair, P. R., Sinclair, J. F., Bonkowsky, H. L., et al. (1982) · Biochemical Pharmacology · doi:10.1016/0006-2952(82)90333-1 · Cited by 27 · see citing works
Burke, P. V., Kwast, K. E., Everts, F., & Poyton, R. Ο. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.3.1040-1044.1998 · Cited by 19 · see citing works
Self-citationKwast, K. E., Burke, P. V., Brown, K., et al. (1997) · Current Genetics · doi:10.1007/s002940050291 · Cited by 18 · see citing works
Self-citationCytochrome Oxidase is the Primary Oxygen Sensor in the Cat Carotid Body
Lahiri, S., Chugh, D. K., Mokashi, A., et al. (1996) · Advances in experimental medicine and biology · doi:10.1007/978-1-4613-0333-6_26 · Cited by 6 · see citing works
Export of Proteins from Mitochondria
Poyton, R. Ο., Sevarino, K. A., McKee, E. E., et al. (1996) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(09)60017-5 · Cited by 5 · see citing works
Self-citationHeme-Mediated Gene Regulation in Saccharomyces cerevisiae
Pinkham, J. L., & Keng, T. (2020) · CRC Press eBooks · doi:10.1201/9781003067221-16 · Cited by 3 · see citing works
Flagged first, then by citations
Research works printed but not linked: 12
- [9]Acker H, Xue D. News Physiol Sci. 1995;10:211–215. [Google Scholar]
- [23]Poyton R O, Burke P V. Biochim Biophys Acta. 1992;1101:252–256. [PubMed] [Google Scholar]
- [27]Waterland R A, Basu A, Chance B, Poyton R O. J Biol Chem. 1991;266:4180–4186. [PubMed] [Google Scholar]
- [30]Tzagoloff A, Akai A, Needleman R B, Zulch G. J Biol Chem. 1975;250:8236–8242. [PubMed] [Google Scholar]
- [33]Tsang S S, Yin X, Guzzzo-Arkuran C, Jones V S, Davison A J. BioTechniques. 1993;14:380–381. [PubMed] [Google Scholar]
- [38]Goldberg M A, Schneider T J. J Biol Chem. 1994;269:4355–4359. [PubMed] [Google Scholar]
- [45]Yonetoni T, Yamamoto H, Woodrow G V. J Biol Chem. 1974;249:682–690. [PubMed] [Google Scholar]
- [48]Linnane A W, Haslam J M. Curr Top Cell Regul. 1970;2:101–172. [Google Scholar]
- [49]Lahiri S. News Physiol Sci. 1994;9:161–165. [Google Scholar]
- [50]Wilson D F, Rumsey W L, Green T J, Vanderkooi J M. J Biol Chem. 1988;263:2712–2718. [PubMed] [Google Scholar]
- [52]Rumsey W L, Schlosser C, Nuutinen E M, Robiolio M, Wilson D F. J Biol Chem. 1990;265:15392–15399. [PubMed] [Google Scholar]
- [61]Poyton R O, Sevarino K A, McKee E E, Duhl D J M, Cameron V, Goehring B. Adv Mol Cell Biol. 1996;17:247–280. [Google Scholar]
Cited by
Sorted by citations
Castello, P. R., David, P. S., McClure, T., Crook, Z., & Poyton, R. O. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.011 · Cited by 495 · see citing works
Self-citationRegulation of Ergosterol Biosynthesis in Saccharomyces cerevisiae
Jordá, T., & Puig, S. (2020) · Genes · doi:10.3390/genes11070795 · Cited by 489 · see citing works
Perspectives on Oxygen Sensing
Semenza, G. L. (1999) · Cell · doi:10.1016/s0092-8674(00)81957-1 · Cited by 385 · see citing works
Willger, S. D., Puttikamonkul, S., Kim, K.-H., Burritt, J. B., Grahl, N., Metzler, L. J., Barbuch, R., Bard, M., Lawrence, C. B., & Cramer, R. A. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000200 · Cited by 345 · see citing works
Foury, F., & Roganti, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111789200 · Cited by 171 · see citing works
Rosenfeld, E., & Beauvoit, B. (2003) · Yeast · doi:10.1002/yea.1026 · Cited by 149 · see citing works
Abramova, N. E., Cohen, B. D., Sertil, O., Kapoor, R., Davies, K. J. A., & Lowry, C. V. (2001) · Genetics · doi:10.1093/genetics/157.3.1169 · Cited by 128 · see citing works
A Role for Sterol Levels in Oxygen Sensing in <i>Saccharomyces cerevisiae</i>
Davies, B. S. J., & Rine, J. (2006) · Genetics · doi:10.1534/genetics.106.059964 · Cited by 123 · see citing works
Castello, P. R., Woo, D. K., Ball, K., Wojcik, J., Liu, L., & Poyton, R. O. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709461105 · Cited by 121 · see citing works
Self-citationCellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis
Hausmann, A., Samans, B., Lill, R., & Mühlenhoff, U. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705570200 · Cited by 111 · see citing works
Grahl, N., Dinamarco, T. M., Willger, S. D., Goldman, G. H., & Cramer, R. A. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08034.x · Cited by 99 · see citing works
Jiang, Y., Vasconcelles, M. J., Wretzel, S., Light, A., Martin, C. E., & Goldberg, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6161-6169.2001 · Cited by 95 · see citing works
Hillmann, F., Linde, J., Beckmann, N., Cyrulies, M., Strassburger, M., Heinekamp, T., Haas, H., Guthke, R., Kniemeyer, O., & Brakhage, A. A. (2014) · Molecular Microbiology · doi:10.1111/mmi.12679 · Cited by 26 · see citing works
A role for MGA2, but not SPT23, in activation of transcription of ERG1 in Saccharomyces cerevisiae
Rice, C., Cooke, M., Treloar, N., Vollbrecht, P., Stukey, J., & McDonough, V. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.11.020 · Cited by 12 · see citing works
- Authors
- Kwast, K. E., Burke, P. V., Staahl, B. T., & Poyton, R. O.
- Affiliations
- University of Colorado Boulder (US)
- Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309-0347
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1999-05-11
- Volume
- 96
- Issue
- 10
- Pages
- 5446-5451
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC21879
- OpenAlex
- W2168009569
- Cited by
- 175
- References
- 66
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 2 · 2023: 4 · 2021: 4 · 2020: 5 · 2019: 5 · 2018: 3 · 2017: 4 · 2016: 3 · 2015: 3 · 2014: 4 · 2013: 8 · 2012: 12
- FWCI
- 3.91
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM 30228, R01GM030228)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- oxygen sensing, hypoxic gene expression, Saccharomyces cerevisiae, cytochrome c oxidase, flavohemoglobin, carbon monoxide, electron transport chain, heme, OLE1, COX5B, cobalt, nickel, anoxia, transcriptional regulation
- MeSH terms
- Aerobiosis, Antimycin A, Carbon Monoxide, Cobalt, Cytochrome c Group, Electron Transport Complex IV, Genes, Fungal, Hemeproteins, Mutation, Nickel, Oxygen, Potassium Cyanide, RNA, Messenger, Saccharomyces cerevisiae, Stearoyl-CoA Desaturase, Gene Expression Regulation, Fungal, Fatty Acid Desaturases, Cytochromes c
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