The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
Abstract
Heat shock promoters contain one or more binding sites for a specific heat shock factor (HSF). We report the cloning and sequence of the gene encoding yeast HSF, and demonstrate that HSF is required for growth at normal temperatures (15 degrees C-30 degrees C). The activity of a promoter containing a synthetic HSF binding site varies over a 200-fold range between 15 degrees C and 39 degrees C (heat shock). This change in activity is accompanied by multiple changes in the phosphorylation state of HSF, but all forms of HSF are able to bind DNA. We propose that the expression of heat shock genes in yeast is modulated by phosphorylation of DNA-bound HSF, and that this leads to a more efficient interaction of the factor with other components of the transcriptional machinery.
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“Hsf1 is activated by hyperphosphorylation in response to specific environmental cues, which in some fungi include glucose starvation, superoxide, oxygen tension and changes in membrane lipid composition as well as heat shock10,39,45,46.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [39]
In the citing paper
“Hsf1 is essential for viability in yeasts10,38,39, and is required for the basal expression of HSP genes10,39,40.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [39]
Citations
Cites
Lindquist, S. L. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.005443 · Cited by 4,611
A short amino acid sequence able to specify nuclear location
Kalderon, D., Roberts, B., Richardson, W. D., & Smith, A. E. (1984) · Cell · doi:10.1016/0092-8674(84)90457-4 · Cited by 2,511
Supercoil Sequencing: A Fast and Simple Method for Sequencing Plasmid DNA
Chen, E. Y., & Seeburg, P. H. (1985) · DNA · doi:10.1089/dna.1985.4.165 · Cited by 2,388
Boeke, J. D., Lacroute, F., & Fink, G. R. (1984) · Molecular and General Genetics MGG · doi:10.1007/bf00330984 · Cited by 2,354
70K heat shock related proteins stimulate protein translocation into microsomes
Chirico, W. J., Waters, M. G., & Blobel, G. (1988) · Nature · doi:10.1038/332805a0 · Cited by 1,232
Yeast RNA Polymerase II Genes: Isolation with Antibody Probes
Young, R. A., & Davis, R. W. (1983) · Science · doi:10.1126/science.6356359 · Cited by 1,077
Sequences That Regulate the Divergent GAL1-GAL10 Promoter in Saccharomyces cerevisiae
Johnston, M., & Davis, R. W. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.8.1440-1448.1984 · Cited by 980
Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of Yeast
Hope, I. A., & Struhl, K. (1986) · Cell · doi:10.1016/0092-8674(86)90070-x · Cited by 918
Deletion analysis of GAL4 defines two transcriptional activating segments
Ma, J., & Ptashne, M. (1987) · Cell · doi:10.1016/0092-8674(87)90081-x · Cited by 887
Craig, E. A., & Schlesinger, M. J. (1985) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238509085135 · Cited by 809
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Mitchell, P. J., & Tjian, R. (1989) · Science · doi:10.1126/science.2667136 · Cited by 3,046
The biochemistry and medical significance of the flavonoids
Havsteen, B. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00298-x · Cited by 2,702
Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.24.3788 · Cited by 1,898
Candida albicans pathogenicity mechanisms
Mayer, F. L., Wilson, D., & Hube, B. (2013) · Virulence · doi:10.4161/viru.22913 · Cited by 1,848
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
Ciocca, D. R., & Calderwood, S. K. (2005) · Cell Stress and Chaperones · doi:10.1379/csc-99r.1 · Cited by 1,420
Schlesinger, M. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38314-0 · Cited by 1,362
The regulation of transcription by phosphorylation
Hunter, T. R., & Karin, M. (1992) · Cell · doi:10.1016/0092-8674(92)90162-6 · Cited by 1,273
The DNA-dependent protein kinase: Requirement for DNA ends and association with Ku antigen
Gottlieb, T. M., & Jackson, S. P. (1993) · Cell · doi:10.1016/0092-8674(93)90057-w · Cited by 1,233
The plant heat stress transcription factor (Hsf) family: Structure, function and evolution
Scharf, K., Berberich, T., Ebersberger, I., & Nover, L. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.10.002 · Cited by 1,159
Boyle, W. J., Smeal, T., Defize, L. H. K., Angel, P. E., Woodgett, J. R., Karin, M., & Hunter, T. R. (1991) · Cell · doi:10.1016/0092-8674(91)90241-p · Cited by 1,039
Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
Pirkkala, L., NYKÄNEN, P., & Sistonen, L. (2001) · The FASEB Journal · doi:10.1096/fj00-0294rev · Cited by 996
Norman, C. M., Runswick, M. J., Pollock, R. M., & Treisman, R. (1988) · Cell · doi:10.1016/0092-8674(88)90244-9 · Cited by 933
Sarge, K. D., Murphy, S. P., & Morimoto, R. I. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.3.1392 · Cited by 883
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
Morimoto, R. I. (2008) · Genes & Development · doi:10.1101/gad.1657108 · Cited by 872
Transcriptional Regulator of Oxidative Stress-Inducible Genes: Direct Activation by Oxidation
Storz, G., Tartaglia, L. A., & Ames, B. N. (1990) · Science · doi:10.1126/science.2183352 · Cited by 864
Benjamin, I. J., & McMillan, D. R. (1998) · Circulation Research · doi:10.1161/01.res.83.2.117 · Cited by 840
Regulation of H SF 1 Function in the Heat Stress Response: Implications in Aging and Disease
Anckar, J., & Sistonen, L. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060809-095203 · Cited by 811
&cestflwr; The Hsp90 family of proteins in Arabidopsis thaliana
Krishna, P., & Gloor, G. B. (2001) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2001)006 · Cited by 360
A novel octamer binding transcription factor is differentially expressed in mouse embryonic cells
Okamoto, K., Okazawa, H., Okuda, A., Sakai, M., Muramatsu, M., & Hamada, H. (1990) · Cell · doi:10.1016/0092-8674(90)90597-8 · Cited by 723
Charng, Y., Liu, H., Liu, N.-Y., Chi, W.-T., Wang, C., Chang, S.-H., & Wang, T.-T. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.091322 · Cited by 693
Tanaka, M., & Herr, W. (1990) · Cell · doi:10.1016/0092-8674(90)90589-7 · Cited by 625
Mā, H., Yanofsky, M. F., & Meyerowitz, E. M. (1991) · Genes & Development · doi:10.1101/gad.5.3.484 · Cited by 623
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Sorger, P. K. (1991) · Cell · doi:10.1016/0092-8674(91)90452-5 · Cited by 603
Self-citationA regulatory hierarchy for cell specialization in yeast
Herskowitz, I. (1989) · Nature · doi:10.1038/342749a0 · Cited by 590
Verghese, J., Abrams, J., Wang, Y., & Morano, K. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05018-11 · Cited by 575
Xiao, X., Zuo, X., Davis, A. A., McMillan, D. R., Curry, B. B., Richardson, J. A., & Benjamin, I. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5943 · Cited by 542
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Rabindran, S. K., Haroun, R. I., Clos, J., Wiśniewski, J., & Wu, C. (1993) · Science · doi:10.1126/science.8421783 · Cited by 489
Kamada, Y., Jung, U. S., Piotrowski, J., & Levin, D. E. (1995) · Genes & Development · doi:10.1101/gad.9.13.1559 · Cited by 488
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Miller, G., & Mittler, R. (2006) · Annals of Botany · doi:10.1093/aob/mcl107 · Cited by 484
Schmitt, A. P., & McEntee, K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5777 · Cited by 472
Hanes, S. D., & Brent, R. (1989) · Cell · doi:10.1016/0092-8674(89)90063-9 · Cited by 464
Stress tolerance: The key to effective strains of industrial baker's yeast
Attfield, P. V. (1997) · Nature Biotechnology · doi:10.1038/nbt1297-1351 · Cited by 461
Baler, R., Dahl, G., & Voellmy, R. W. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2486 · Cited by 460
Molecular cloning and expression of a human heat shock factor, HSF1.
Rabindran, S. K., Giorgi, G., Clos, J., & Wu, C. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.6906 · Cited by 456
The liver-specific transcription factor LF-B1 contains a highly diverged homeobox DNA binding domain
Frain, M., Swart, G. W. M., Monaci, P., Nicosia, A., Stämpfli, S., Frank, R. W., & Cortese, R. (1989) · Cell · doi:10.1016/0092-8674(89)90877-5 · Cited by 454
Genome-Wide Analysis of the Biology of Stress Responses through Heat Shock Transcription Factor
Hahn, J., Hu, Z., Thiele, D. J., & Iyer, V. R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.12.5249-5256.2004 · Cited by 438
Role of the AMP-activated protein kinase in the cellular stress response
Corton, J. M., Gillespie, J. G., & Hardie, D. G. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00070-1 · Cited by 423
Transcriptional regulation of heat shock genes. A paradigm for inducible genomic responses.
Morimoto, R. I., Sarge, K. D., & Abravaya, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41621-3 · Cited by 416
Perišić, O., Xiao, H., & Lis, J. T. (1989) · Cell · doi:10.1016/0092-8674(89)90603-x · Cited by 411
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Morimoto, R. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2012.76.010637 · Cited by 419
Ruis, H., & Schüller, C. (1995) · BioEssays · doi:10.1002/bies.950171109 · Cited by 406
Effect of Sodium Salicylate on the Human Heat Shock Response
Jurivich, D. A., Sistonen, L., Kroes, R. A., & Morimoto, R. I. (1992) · Science · doi:10.1126/science.1546322 · Cited by 395
Chu, B., Soncin, F., Price, B. D., Stevenson, M. A., & Calderwood, S. K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30847 · Cited by 382
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Sorger, P. K., & Nelson, H. C. M. (1989) · Cell · doi:10.1016/0092-8674(89)90604-1 · Cited by 376
Self-citationStress-induced oligomerization and chromosomal relocalization of heat-shock factor
Westwood, J. T., Clos, J., & Wu, C. (1991) · Nature · doi:10.1038/353822a0 · Cited by 370
Sarge, K. D., Zimarino, V., Holm, K., Wu, C., & Morimoto, R. I. (1991) · Genes & Development · doi:10.1101/gad.5.10.1902 · Cited by 367
Clos, J., Westwood, J. T., Becker, P. B., Wilson, S. E., Lambert, K. N., & Wu, C. (1990) · Cell · doi:10.1016/0092-8674(90)90511-c · Cited by 359
Nakai, A., Tanabe, M., Kawazoe, Y., Inazawa, J., Morimoto, R. I., & Nagata, K. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.1.469 · Cited by 351
Stress-induced transcriptional activation
Mager, W. H., & Kruijff, A. J. D. (1995) · Microbiological Reviews · doi:10.1128/mr.59.3.506-531.1995 · Cited by 351
Schramm, F., Ganguli, A., Kiehlmann, E., Englich, G., Walch, D., & von Koskull‐Döring, P. (2006) · Plant Molecular Biology · doi:10.1007/s11103-005-5750-x · Cited by 348
Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans.
Schuetz, T. J., Gallo, G. J., Sheldon, L. A., Tempst, P., & Kingston, R. E. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.6911 · Cited by 339
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Franke, A., DeCamillis, M. A., Zink, D., Cheng, N., Brock, H. W., & Paro, R. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05364.x · Cited by 330
Kotak, S., Vierling, E., Bäumlein, H., & von Koskull‐Döring, P. (2007) · The Plant Cell · doi:10.1105/tpc.106.048165 · Cited by 324
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Guettouche, T., Boellmann, F., Lane, W. S., & Voellmy, R. W. (2005) · BMC Biochemistry · doi:10.1186/1471-2091-6-4 · Cited by 328
Kline, M. P., & Morimoto, R. I. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.4.2107 · Cited by 312
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Ding, J., Huang, X., Zhang, L., Zhao, N., Yang, D., & Zhang, K. (2009) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-009-2223-1 · Cited by 309
Scharf, K., Rose, S., Zott, W., Schöffl, F., Nover, L., & Schöff, F. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07900.x · Cited by 306
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Bauer, F. F., & Pretorius, I. S. (2000) · South African Journal of Enology and Viticulture · doi:10.21548/21-1-3557 · Cited by 284
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Heat shock proteins, thermotolerance, and their relevance to clinical hyperthermia
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Chaperone Regulation of the Heat Shock Protein Response
Voellmy, R. W., & Boellmann, F. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1_9 · Cited by 267
Yamada, K., Fukao, Y., Hayashi, M., Fukazawa, M., Suzuki, I., & Nishimura, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707168200 · Cited by 251
Dynamic control of Hsf1 during heat shock by a chaperone switch and phosphorylation
Zheng, X., Krakowiak, J., Patel, N., Ali Beyzavi, B., Ezike, J., Khalil, A. S., & Pincus, D. (2016) · eLife · doi:10.7554/elife.18638 · Cited by 249
Moses, K., & Rubin, G. M. (1991) · Genes & Development · doi:10.1101/gad.5.4.583 · Cited by 243
The heat shock factor family and adaptation to proteotoxic stress
Fujimoto, M., & Nakai, A. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07827.x · Cited by 251
Sorger, P. K. (1990) · Cell · doi:10.1016/0092-8674(90)90123-v · Cited by 241
Self-citationÖstling, P., Björk, J., Roos‐Mattjus, P., Mezger, V., & Sistonen, L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607556200 · Cited by 238
Cooperative binding of drosophila heat shock factor to arrays of a conserved 5 bp unit
Xiao, H., Perišić, O., & Lis, J. T. (1991) · Cell · doi:10.1016/0092-8674(91)90242-q · Cited by 238
Chou, S., Prince, T. L., Gong, J., & Calderwood, S. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039679 · Cited by 228
Negative regulation of the heat shock transcriptional response by HSBP1Preprint
Satyal, S. H., Chen, D., Fox, S. G., Kramer, J. M., & Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.13.1962 · Cited by 225
Activation domains of stably bound GAL4 derivatives alleviate repression of promoters by nucleosomes
Workman, J. L., Taylor, I. C. A., & Kingston, R. E. (1991) · Cell · doi:10.1016/0092-8674(91)90237-s · Cited by 224
Trott, A. E., West, J. D., Klaić, L., Westerheide, S. D., Silverman, R. B., Morimoto, R. I., & Morano, K. A. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1004 · Cited by 223
Heat-shock protein 104 expression is sufficient for thermotolerance in yeast.
Lindquist, S., & Kim, G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5301 · Cited by 223
Chauhan, H., Khurana, N., Agarwal, P., & Khurana, P. (2011) · Molecular Genetics and Genomics · doi:10.1007/s00438-011-0638-8 · Cited by 218
Inhibition of the Activation of Heat Shock Factor In Vivo and In Vitro by Flavonoids
Hosokawa, N., Hirayoshi, K., Kudo, H., Takechi, H., Aoike, A., Kawai, K., & Nagata, K. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.8.3490 · Cited by 218
Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers.Preprint
Berberich, S. J., & Cole, M. D. (1992) · Genes & Development · doi:10.1101/gad.6.2.166 · Cited by 218
Westwood, J. T., & Wu, C. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3481 · Cited by 213
The DNA-Binding Activity of the Human Heat Shock Transcription Factor Is Regulated In Vivo by hsp70
Mosser, D. D., Duchaine, J., & Bernard Massie, B. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.9.5427-5438.1993 · Cited by 211
Hepatitis B virus X‐gene product: A promiscuous transcriptional activator
Rossner, M. T. (1992) · Journal of Medical Virology · doi:10.1002/jmv.1890360207 · Cited by 211
Heat stress proteins and transcription factors
Nover, L., & Scharf, K. (1997) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000583 · Cited by 210
Mager, W. H., & Ferreira, P. M. (1993) · Biochemical Journal · doi:10.1042/bj2900001 · Cited by 204
Wagner, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4387 · Cited by 204
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Inducibility of the response of yeast cells to peroxide stress
Collinson, L. P., & Dawes, I. W. (1992) · Journal of General Microbiology · doi:10.1099/00221287-138-2-329 · Cited by 202
Roles of heat shock factor 1 beyond the heat shock response
Barna, J., Csermely, P., & Vellai, T. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2836-6 · Cited by 214
Metadata
- Authors
- Sorger, P. K., & Pelham, H. R. B.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1988-09
- Volume
- 54
- Issue
- 6
- Pages
- 855-864
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2005131012
- Cited by
- 832
- References
- 27
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 12 · 2023: 6 · 2022: 21 · 2021: 10 · 2020: 16 · 2019: 11 · 2018: 15 · 2017: 10 · 2016: 22 · 2015: 9 · 2014: 15 · 2013: 25 · 2012: 17
- FWCI
- 24.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- heat shock transcription factor, Saccharomyces cerevisiae, heat shock promoter, protein phosphorylation, DNA binding, heat shock gene expression, transcriptional regulation, gene cloning
- MeSH terms
- Amino Acid Sequence, Base Sequence, Cell Survival, Cloning, Molecular, DNA-Binding Proteins, Gene Expression Regulation, Hot Temperature, Heat-Shock Proteins, Molecular Sequence Data, Molecular Weight, Phosphoproteins, Phosphorylation, Saccharomyces cerevisiae, Transcription Factors, Transcription, Genetic
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