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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Cited by
Sorted by citations
Items 701–800 of 806
Biochemical events in the activation and attenuation of the heat shock transcriptional response
Satyal, S. H., & Morimoto, R. I. (1998) · Journal of Biosciences · doi:10.1007/bf02936123 · Cited by 4
Mizoguchi, H., & Hara, S. (2001) · Journal of Bioscience and Bioengineering · doi:10.1016/s1389-1723(01)80107-9 · Cited by 4
Surprising features of transcriptional regulation of heat shock genes.
Sarge, K. D., & Morimoto, R. I. (1991) · Europe PMC (PubMed Central) · Cited by 4
The Heat-Shock Response: Sensing the Stress of Misfolded Proteins
Morimoto, R. I., & Nollen, E. A. A. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50672-0 · Cited by 4
The Heat Shock Response and Transplantation Immunology
Wheeler, D. S., & Wong, H. R. (2004) · Springer eBooks · doi:10.1007/978-1-4419-8999-4_29 · Cited by 4
Horta, M. F., Fu, K. C., Koizumi, H., Young, J. D., & Liu, C. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0639w.x · Cited by 4
Km, C., Ja, H.-Z., & Jacob, S. T. (1991) · Europe PMC (PubMed Central) · Cited by 4
Hu, J., Li, Y., Wu, S., Liu, L., Zhou, J., Li, W., Zhang, R., Liang, Z., Yang, D., & 杨, Z. Q. 梓. Y. (2026) · Genes · doi:10.3390/genes17040473 · Cited by 3
Heat Shock Proteins and Cancer
Nagaraja, G. M., & Asea, A. A. A. (2009) · Heat shock proteins · doi:10.1007/978-90-481-3381-9_7 · Cited by 3
Xu, F., Wang, W., Chen, L., Liu, Q., Qiu, H., Muraleedharan, V., Zhou, B., Cheng, H., Huang, Z., Weian, X., et al. (2012) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-1193-7 · Cited by 3
Analysis of in vivo binding of yeast heat shock factor to promoter DNA
Liu, K., Zhang, L., Ding, X., Deng, B., & Chen, W. (2008) · AFRICAN JOURNAL OF BIOTECHNOLOGY · doi:10.4314/ajb.v7i8.58622 · Cited by 3
Mechanism of High Alcoholic Fermentation Ability of Sake Yeast
Watanabe, D., Takagi, H., & Shimoi, H. (2015) · Springer eBooks · doi:10.1007/978-4-431-55248-2_4 · Cited by 3
Nollen, E. A. A., & Morimoto, R. I. (2002) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm1261 · Cited by 3
Wang, Y., Ma, Z., Li, G., Meng, X., Duan, S., Liu, Z., Zhao, M., Guo, X., & Zhang, H. (2025) · Plants · doi:10.3390/plants14131950 · Cited by 2
Molecular Chaperones and HSPs in Sugarcane and Eucalyptus
Gonçalves, C. C., & Ramos, C. H. I. (2016) · Heat shock proteins · doi:10.1007/978-3-319-46340-7_13 · Cited by 2
Crosstalk Between Osmolytes and Cellular Chaperones: Examples in Saccharomyces cerevisiae
Pallapati, A., Das, E., & Roy, I. (2017) · Springer eBooks · doi:10.1007/978-981-10-3707-8_3 · Cited by 2
Singh, G., Banerjee, G., Sarkar, N. K., Sinha, A. K., & Grover, A. (2022) · Physiologia Plantarum · doi:10.1111/ppl.13754 · Cited by 2
Unfolded protein responses in Chlamydomonas reinhardtii
Gabelmann, S., & Schroda, M. (2025) · Biological Chemistry · doi:10.1515/hsz-2025-0101 · Cited by 2
Prinz, B., & Lang, C. (2004) · Springer eBooks · doi:10.1007/978-3-662-07426-8_8 · Cited by 2
Introduction: Heat Shock Proteins—From Drosophila Stress Proteins to Mediators of Human Disease
Calderwood, S. K. (2007) · Springer eBooks · doi:10.1007/978-0-387-39717-7_1 · Cited by 2
Heat Shock Factor (HSF): The Promoter of Chaperone Genes. A Mini Review
Quel, N. G., & Ramos, C. H. I. (2018) · Current Proteomics · doi:10.2174/1570164615666180713095309 · Cited by 2
RNA Polymerases and Transcription Factors
Tyler, B. M., & Holland, M. J. (1996) · Springer eBooks · doi:10.1007/978-3-662-10367-8_5 · Cited by 2
Autoregulation of the Heat Shock Response
Shi, Y., & Morimoto, R. I. (1999) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-58259-2_10 · Cited by 2
Sadhale, P. P., Sharma, N., Beena, P. S., Katoch, A., Acharya, N., & Singh, S. K. (1998) · Journal of Biosciences · doi:10.1007/bf02936125 · Cited by 2
Cloning and sequencing of heat shock factor (HSF1) cDNA from human retina
Pardhasaradhi, K., Kutty, R. K., Park, C. S., & Krishna, G. A. (1994) · Current Eye Research · doi:10.3109/02713689409047008 · Cited by 2
An Alteration in Molecular Form Associated with Activation of Human Heat Shock Factor.
Kimura, Y., Taniguchi, T., & Yahara, I. (1991) · Cell Structure and Function · doi:10.1247/csf.16.263 · Cited by 2
Phosphorylation of Nuclear Proteins in Myelinating Oligodendrocytes and Its Control by Cyclic AMP
Sato‐Bigbee, C., & Yu, R. K. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb06364.x · Cited by 2
Functional analysis of the Saccharomyces cerevisiae UBC11 gene
Townsley, F. M., & RUDERMAN, J. V. (1998) · Yeast · doi:10.1002/(sici)1097-0061(19980615)14:8 · Cited by 24
Abbaraju, H. R., Behal, R. H., & Oliver, D. J. (2002) · Journal of Plant Biochemistry and Biotechnology · doi:10.1007/bf03263138 · Cited by 2
Transcriptional re-wiring by mutation of the yeast Hsf1 oligomerization domainPreprint
Morton, E. A., Dorrity, M. W., Zhou, W. Y., Fields, S., & Queitsch, C. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.23.112250 · Cited by 2
Structure and Function of Drosophila Heat Shock Factor
Wu, C., Clos, J., Westwood, J. T., Zimarino, V., Becker, P. B., & Wilson, S. E. (1991) · Springer eBooks · doi:10.1007/978-3-642-76679-4_2 · Cited by 2
The molecular logic of Gtr1/2- and Pib2-dependent TORC1 regulation in budding yeastPreprint
Cecil, J. H., Padilla, C. M., Lipinski, A. A., Langlais, P. R., Luo, X., & Capaldi, A. P. (2024) · eLife · doi:10.7554/elife.94628 · Cited by 2
Moallem, M., McNeil, J. B., Bergey, B. G., & Rosonina, E. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag495 · Cited by 1
Role of Antioxidant Systems and Heat Shock Response in Aquatic Animals Under Multistress Conditions
Feidantsis, K. G., Minari, M. D. L., Cubillos, V. M., Dijkstra, P. D., Buzinski, O. D., Moreira, D. C., & Hermes‐Lima, M. (2026) · Antioxidants · doi:10.3390/antiox15080917 · Cited by 1
Schöffl, F., Hübel, A., & Lee, J. H. (1996) · Springer eBooks · doi:10.1007/978-3-642-61175-9_4 · Cited by 1
Role and regulatory mechanisms of heat shock factor 2
Björk, J. (2011) · Cited by 1
Role of Heat Shock Protein 90 in Diabetes and Pancreatic Cancer Management
Sushma, P. S., Momin, S., & Srivani, G. (2019) · Springer eBooks · doi:10.1007/978-981-32-9393-9_11 · Cited by 1
Znaidi, S. (2024) · mSphere · doi:10.1128/msphere.00644-23 · Cited by 2
Establishing the microcrustacean Daphnia as a model system for research on aging
Schumpert, C. A. (2015) · Scholar Commons (University of South Carolina) · Cited by 1
Basic techniques for transgenesis
Wilmut, I., & Clark, A. J. (2019) · Bioscientifica Proceedings · doi:10.1530/biosciprocs.2.021 · Cited by 1
Regulation of heat shock factor 1 (HSF1) DNA-binding and transcription
Mercier, P. A. (2003) · University Library - University of Saskatchewan (University of Saskatchewan) · Cited by 1
Lee, Y. J., Galoforo, S., Berns, C. M., Blackburn, R. V., Huberman, E., & Corry, P. M. (1996) · Biochemical Pharmacology · doi:10.1016/0006-2952(96)00209-2 · Cited by 1
Wang, Y. (2012) · Digital Commons-TMC (Texas Medical Center) · Cited by 1
Changes in chromatin proteins during optic nerve regeneration in the goldfish
Gossels, J. M., Lewis, S. E., Perrone-Bizzozero, N., & Benowitz, L. I. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490330114 · Cited by 1
Maresca, B., Lallo, G. D., Pardini, C. L., Petrella, G., & Carratù, L. (1993) · Springer eBooks · doi:10.1007/978-3-642-84625-0_26 · Cited by 1
Isolation and expression of cDNA sequences encoding ovine follicle-stimulating hormone
Mountford, P. S. (1991) · Minerva Access (University of Melbourne) · Cited by 1
Identification of Heat- Shock Factor Regulated Genes and Pathways
Panikulangara, T. J., Busch, W., Kumar, M., & Schöffl, F. (2006) · CRC Press eBooks · doi:10.1201/9780849330636.ch10 · Cited by 1
The complex evolution of the metazoan HSP70 gene familyPreprint
Yu, E.-M., Yoshinaga, T., Jalufka, F. L., Ehsan, H., Welch, D. B. M., & Kaneko, G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.21.307264 · Cited by 1
Joshi, N., Joshi, N., & Börner, G. V. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.09.692842 · Cited by 1
Olsson, B. (2005) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1
Physiological architecture and evolutionary origins of cellular adaptabilityPreprint
Dea, A., Lan, Y., Doran, B. A., Ali, A., Igarashi, M. G., Dyer, L., Aksianiuk, V., Pincus, D., & Raman, A. S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.10.717775 · Cited by 1
Rocha, N. C. A. (2013) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Talbot, D. R., Nagao, R. T., & Pell, E. J. (1991) · Springer eBooks · doi:10.1007/978-1-4612-3060-1_15
Therapeutics: Harnessing the Power of Molecular and Pharmacological Chaperones
Gross, D. S., Klein, R. L., & Witt, S. N. (2011) · Wiley eBooks · doi:10.1002/9781118063903.ch12
Chapter 13 The human heat shock response
Jurivich, D. A. (1996) · Principles of medical biology · doi:10.1016/s1569-2582(96)80138-3
Regulation of heat shock response in yeast and mammalian cells
Seppä, L. (2005) · Työväentutkimus Vuosikirja
Regulation and dymanic behavior of the heat shock transcription factor HSF-1 in C. elegans
Morton, E. A. (2013) · Scholarly Commons (University of Pennsylvania)
Regulation of HSF2 and its function in mitosis
Elsing, A. N. (2014) · Doria (University of Helsinki)
Vihervaara, A. (2014) · Doria (University of Helsinki)
Phosphorylation of the androgen receptor in a human prostate tumor cell line
van Laar, J. H. (1991)
Voellmy, R. W. (2007) · Springer eBooks · doi:10.1007/978-0-387-39717-7_6
Jones, T. J. (2004) · OhioLink ETD Center (Ohio Library and Information Network)
Expressão, regulação e funcionalidade de genes HSPs no dermatófito Trichophyton rubrum
Jacob, T. R. (2016) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.17.2016.tde-15052014-105536
Schilirò, E. (2000) · Kölner Universitäts PublikationsServer (Universität zu Köln)
The identification of novel regulatory elements in the promoters of heat shock response genes
Ncube, S. (2010) · University of the Western Cape Electronic Theses and Dissertations Repository (University of the Western Cape)
Regulation of transcriptional activation in response to heat stress and osmostress
Roig, C. R. (2011) · Repositori digital de la UPF (Universitat Pompeu Fabra)
Regulation of Hsp70 function by nucleotide-exchange factors
Gowda, N. K. C. (2016) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
The role of TbZC3H11 in the trypanosomal heat shock response
Droll, D. (2012) · heiDOK (Heidelberg University) · doi:10.11588/heidok.00013829
Identification of Heat Shock Factor Binding Sites in the Drosophila Genome
Gonsalves, S. E. (2012) · TSpace (University of Toronto)
Análise do efeito da superexpressão de HSP27 humana na longevidade de Saccharomyces cerevisiae.
Camandona, V. D. L. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.87.2019.tde-06122018-092044
Kim, H. (2008) · Corpus Université Laval (Université Laval)
Transcriptional Regulation of the Interferon Genes
MacDonald, N. J. (1990) · Enlighten: Theses (The University of Glasgow)
Investigating phase separation mechanisms for transcriptional control
Boehning, M. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8312
Proteostasis beyond chaperones - Auxiliary systems in the management of damaged proteins
Josefson, R. (2021) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Sierra, F. (1990) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-6383-4_7
Biochemie und Molekularbiologie 1988
(1989) · Nachrichten aus Chemie Technik und Laboratorium · doi:10.1002/nadc.19890370210
Lang‐Hinrichs, C. (1995) · Springer eBooks · doi:10.1007/978-3-662-10364-7_9
Identification of Heat- Shock Factor Regulated Genes and Pathways
Panikulangara, T. J., Busch, W., Kumar, M., & Schöffl, F. (2006) · CRC Press eBooks · doi:10.1201/9781420004618.ch10
Cowen, L. E., & Leach, M. D. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718151387.793486069
Schnapp, A., Rosenbauer, H., & Grummt, I. (1991) · Springer eBooks · doi:10.1007/978-1-4615-3886-8_17
The Molecular Logic of Gtr1/2 and Pib2 Dependent TORC1 Regulation in Budding YeastPreprint
Cecil, J. H., Padilla, C. M., Lipinski, A. A., Langlais, P. R., Luo, X., & Capaldi, A. P. (2024) · eLife · doi:10.7554/elife.94628.1
Design and application of composite RNA aptamers
Wang, S. (2011) · doi:10.54014/2tyn-fawe
Dzięgielewska, K. M., & Brown, W. M. (1995) · Molecular biology intelligence unit · doi:10.1007/978-3-662-21898-3_4
ETUDE DE LA DEACETYLASE HDAC6 : UNE ENZYME MULTIFONCTIONNELLE
Gilquin, B. (2005) · OpenGrey (Institut de l'Information Scientifique et Technique)
Genetic Models of HSF Function
Orosz, A., & Benjamin, I. J. (2007) · Springer eBooks · doi:10.1007/978-0-387-39717-7_5
He, M., Zhang, K., Zhai, Z., Li, M., Xu, C., Tian, Y., & Liu, L. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6309934
Etude fonctionnelle et inhibition de la protéine Bdf1 chez Candida albicans
Champleboux, M. (2016) · theses.fr (ABES) · doi:10.70675/07079ce8z25e3z45dfz98e6ze8e3ccbc6182
Ciblage thérapeutique de la réponse au stress cellulaire dans l'ostéosarcome
Moukengué, B. (2019) · theses.fr (ABES) · doi:10.70675/26cb2736z4fbdz42d2zabcbzca5db0a782e1
Mitochondrial respiration modulates Hsf1 activation and the heat shock responsePreprint
McDonald, D. W., Dea, A., Sava, R., Kim, Y. J., Joos, L., Pincus, D., & Duennwald, M. L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.07.723568
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review