Cited by 641Heat shock proteins researchFungal and yeast genetics researchUbiquitin and proteasome pathways

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hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

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Borkovich, K A, Farrelly, F W, Finkelstein, D B, Taulien, J, Lindquist, S·1989·Molecular and Cellular Biology

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Abstract

hsp82 is one of the most highly conserved and abundantly synthesized heat shock proteins of eucaryotic cells. The yeast Saccharomyces cerevisiae contains two closely related genes in the HSP82 gene family. HSC82 was expressed constitutively at a very high level and was moderately induced by high temperatures. HSP82 was expressed constitutively at a much lower level and was more strongly induced by heat. Site-directed disruption mutations were produced in both genes. Cells homozygous for both mutations did not grow at any temperature. Cells carrying other combinations of the HSP82 and HSC82 mutations grew well at 25 degrees C, but their ability to grow at higher temperatures varied with gene copy number. Thus, HSP82 and HSC82 constitute an essential gene family in yeast cells. Although the two proteins had different patterns of expression, they appeared to have equivalent functions; growth at higher temperatures required higher concentrations of either protein. Biochemical analysis of hsp82 from vertebrate cells suggests that the protein binds to a variety of other cellular proteins, keeping them inactive until they have reached their proper intracellular location or have received the proper activation signal. We speculate that the reason cells require higher concentrations of hsp82 or hsc82 for growth at higher temperatures is to maintain proper levels of complex formation with these other proteins.

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Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular Cloning. A Laboratory Manual
Wood, E. (1983) · Biochemical Education · doi:10.1016/0307-4412(83)90068-7 · Cited by 29,534
A comprehensive set of sequence analysis programs for the VAX
Devereux, J., Haeberli, P. E., & Smithies, O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.1part1.387 · Cited by 14,222
Transformation of intact yeast cells treated with alkali cations
Ito, H., Fukuda, Y., Murata, K., & Kimura, A. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.163-168.1983 · Cited by 7,518
THE HEAT-SHOCK PROTEINS
Lindquist, S., & Craig, E. A. (1988) · Annual Review of Genetics · doi:10.1146/annurev.ge.22.120188.003215 · Cited by 5,304
Self-citation
[12] One-step gene disruption in yeast
Rothstein, R. J. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)01015-0 · Cited by 3,282
High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules.
Struhl, K., Stinchcomb, D. T., Scherer, S., & Davis, R. W. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.3.1035 · Cited by 1,456
Transformation in yeast: Development of a hybrid cloning vector and isolation of the can1 gene
Broach, J. R., Strathern, J. N., & Hicks, J. B. (1979) · Gene · doi:10.1016/0378-1119(79)90012-x · Cited by 1,073
Principles of protein–protein recognition
Chothia, C., & Janin, J. (1975) · Nature · doi:10.1038/256705a0 · Cited by 1,049
A regulatory upstream promoter element in the Drosophila Hsp 70 heat-shock gene
Pelham, H. R. B. (1982) · Cell · doi:10.1016/0092-8674(82)90249-5 · Cited by 973

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Huang, S., Kuo, Y. H., Lee, W. C., Tsou, H. L., Lee, Y. P., Chang, H. L., Wu, J. J., & Yang, P. C. (1999) · Theriogenology · doi:10.1016/s0093-691x(99)00046-1 · Cited by 77
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Maruya, M., Sameshima, M., Nemoto, T., & Yahara, I. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2349 · Cited by 78
Functional principles and regulation of molecular chaperones
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Lele, Z., Hartson, S. D., Martin, C. C., Whitesell, L. J., Matts, R. L., & Krone, P. H. (1999) · Developmental Biology · doi:10.1006/dbio.1999.9262 · Cited by 74
Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression
Erlejman, A. G., Lagadari, M., Toneatto, J., Piwien‐Pilipuk, G., & Galigniana, M. D. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.12.006 · Cited by 75
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Hsp90—From signal transduction to cell transformation
Brown, M. A., Zhu, L., Schmidt, C., & Tucker, P. W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.054 · Cited by 73
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Nucleotide-Dependent Interaction of Saccharomyces cerevisiae Hsp90 with the Cochaperone Proteins Sti1, Cpr6, and Sba1
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Screening of inbred lines to develop a thermotolerant sunflower hybrid using the temperature induction response (TIR) technique: a novel approach by exploiting residual variability
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Oligomeric forms of the 90-kDa heat shock protein
Nemoto, T., & Sato, N. (1998) · Biochemical Journal · doi:10.1042/bj3300989 · Cited by 71
Purification and characterization of a soluble phosphatidylinositol 4-kinase from the yeast Saccharomyces cerevisiae.
Flanagan, C., & Thorner, J. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35954-4 · Cited by 71
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Wolmarans, A., Lee, B., Spyracopoulos, L., & LaPointe, P. (2016) · Scientific Reports · doi:10.1038/srep33179 · Cited by 72
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Gil, K., Kim, W., Lee, H., Faisal, M., Saquib, Q., Alatar, A. A., & Park, C. (2017) · The Plant Cell · doi:10.1105/tpc.17.00612 · Cited by 70
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Beck, R., Dejeans, N., Glorieux, C., Creton, M., Delaive, E., Dieu, M., Raes, M. J., Levêque, P., Gallez, B., Depuydt, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040795 · Cited by 69
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Wang, Y., & Chen, B. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-20 · Cited by 68
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The Cdc37 protein kinase–binding domain is sufficient for protein kinase activity and cell viability
Lee, P. C., Rao, J., Fliss, A., Yang, E., Garrett, S., & Caplan, A. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200210121 · Cited by 69
Recombinant antibodies: a natural partner in combinatorial antifungal therapy
Matthews, R., & Burnie, J. (2003) · Vaccine · doi:10.1016/j.vaccine.2003.11.032 · Cited by 69
HSP 90 and co‐chaperones: a multitaskers’ view on plant hormone biology
Donato, M. D., & Geisler, M. M. (2019) · FEBS Letters · doi:10.1002/1873-3468.13499 · Cited by 66
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Peffer, S., Gonçalves, D. L., & Morano, K. A. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008822 · Cited by 68
The oxidative stress response of a lager brewing yeast strain during industrial propagation and fermentation
Gibson, B. R., Lawrence, S. J., Boulton, C. A., Box, W. G., Graham, N. S., Linforth, R., & Smart, K. A. (2008) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2008.00371.x · Cited by 67
Heat shock disassembles the nucleolus and inhibits nuclear protein import and poly(A)+ RNA export.
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Basal-Level Expression of the Yeast HSP82 Gene Requires a Heat Shock Regulatory Element
McDaniel, D., Caplan, A. J., Lee, M. S., Adams, C. C., Fishel, B. R., Gross, D. S., & Garrard, W. T. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.11.4789 · Cited by 66
Downregulation of the Hsp90 System Causes Defects in Muscle Cells of Caenorhabditis Elegans
Gaiser, A. M., Kaiser, C. J. O., Haslbeck, V., & Richter, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025485 · Cited by 68
Bacterial infection and tissue-specific Hsp72, -73 and -90 expression in western painted turtles
Ramaglia, V., Harapa, G. M., White, N., & Buck, L. T. (2004) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cca.2004.06.007 · Cited by 65
HSP90 expression correlation with the freezing resistance of bull sperm
Wang, P., Wang, Y., Wang, H., Wang, C., Zan, L., Hu, J., Li, Q., Jia, Y., & Ma, G.-J. (2013) · Zygote · doi:10.1017/s096719941300004x · Cited by 65
Association of heat shock protein 70 with motility of frozen-thawed sperm in bulls
Zhang, X., Hong, J.-Y., Yan, G.-J., Wang, Y.-F., Li, Q.-W., & Hu, J. (2015) · Czech Journal of Animal Science · doi:10.17221/8239-cjas · Cited by 65
Protein chaperones and the heat shock response in Saccharomyces cerevisiae
Morano, K. A., Liu, P. C. C., & Thiele, D. J. (1998) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(98)80011-8 · Cited by 65
Mutational analysis of Hsp90α dimerization and subcellular localization: dimer disruption does not impede ‘in vivo’ interaction with estrogen receptor
Meng, X., Devin, J., Sullivan, W. P., Toft, D. O., Baulieu, É.-É., & CATELLI, M. G. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.7.1677 · Cited by 65
Sensitivity to Hsp90‐targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast
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Mutational analysis of hsp90 binding to the progesterone receptor.
Sullivan, W. P., & Toft, D. O. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80738-8 · Cited by 64
Transcriptional Activation of Heat Shock Protein 90 Mediated Via a Proximal Promoter Region as Trigger of Caspofungin Resistance in Aspergillus fumigatus
Lamoth, F., Juvvadi, P. R., Gehrke, C., Asfaw, Y. G., & Steinbach, W. J. (2014) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit530 · Cited by 62
Developmental Expression of Tomato Heat-Shock Cognate Protein 80
Koning, A. J., Rose, R., & Comai, L. (1992) · PLANT PHYSIOLOGY · doi:10.1104/pp.100.2.801 · Cited by 63
The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range
Girstmair, H., Tippel, F., López, A., Tych, K. M., Stein, F., Haberkant, P., Schmid, P. W. N., Helm, D., Rief, M., Sattler, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11518-w · Cited by 65
Design of improved membrane protein production experiments: Quantitation of the host response
Bonander, N., Hedfalk, K., Larsson, C., Mostad, P., Chang, C., Gustafsson, L., & Bill, R. M. (2005) · Protein Science · doi:10.1110/ps.051435705 · Cited by 62
The Sch9 protein kinase regulates Hsp90 chaperone complex signal transduction activity in vivo
Morano, K. A., & Thiele, D. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5953 · Cited by 62
Contributions of Co-Chaperones and Post-Translational Modifications Towards Hsp90 Drug Sensitivity
Walton‐Diaz, A., Khan, S., Bourboulia, D., Trepel, J. B., Neckers, L., & Mollapour, M. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.88 · Cited by 59
SYM1 Is the Stress-Induced Saccharomyces cerevisiae Ortholog of the Mammalian Kidney Disease Gene Mpv17 and Is Required for Ethanol Metabolism and Tolerance during Heat Shock
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Domain Structures and Immunogenic Regions of the 90-kDa Heat-shock Protein (HSP90)
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In the yeast heat shock response, Hsf1-directed induction of Hsp90 facilitates the activation of the Slt2 (Mpk1) mitogen-activated protein kinase required for cell integrity.
Truman, A. W., Millson, S. H., Nuttall, J. M., Mollapour, M., Prodromou, C., & Piper, P. W. (2007) · Eukaryotic Cell · doi:10.1128/ec.00009-07 · Cited by 59
Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity
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Heat shock protein 90 (Hsp90): A novel antifungal target against Aspergillus fumigatus
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Subcellular localization of the J-protein Sis1 regulates the heat shock response
Feder, Z. A., Ali, A., Singh, A., Krakowiak, J., Zheng, X., Bindokas, V. P., Wolfgeher, D. J., Kron, S. J., & Pincus, D. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202005165 · Cited by 61
Autoregulation of the Heat-Shock Response
Lindquist, S. L. (1993) · Springer eBooks · doi:10.1007/978-1-4615-2894-4_14 · Cited by 57
Self-citation
HtpG Plays a Role in Cold Acclimation in Cyanobacteria
Hossain, M. M., & Nakamoto, H. (2002) · Current Microbiology · doi:10.1007/s00284-001-0005-9 · Cited by 56
Cumulative Impact of Chaperone-Mediated Folding on Genome Evolution
Bogumil, D. D., & Dagan, T. (2012) · Biochemistry · doi:10.1021/bi3013643 · Cited by 56
Heat shock protein 90 is required for sexual and asexual development, virulence, and heat shock response in Fusarium graminearum
Bui, D., Lee, Y., Lim, J. Y., Fu, M., Kim, J.-C., Choi, G. J., Son, H., & Lee, Y. (2016) · Scientific Reports · doi:10.1038/srep28154 · Cited by 57
Function of Cytosolic Chaperones in Tom70-Mediated Mitochondrial Import
C.Y. Fan, A., & C. Young, J. (2011) · Protein & Peptide Letters · doi:10.2174/092986611794475020 · Cited by 64
Structural Basis of the Radicicol Resistance Displayed by a Fungal Hsp90
Prodromou, C., Nuttall, J. M., Millson, S. H., Roe, S. M., Sim, T., Tan, D., Workman, P., Pearl, L. H., & Piper, P. W. (2009) · ACS Chemical Biology · doi:10.1021/cb9000316 · Cited by 56
The Molecular Chaperone Sse1 and the Growth Control Protein Kinase Sch9 Collaborate to Regulate Protein Kinase A Activity in Saccharomyces cerevisiae
Trott, A. E., Shaner, L. M., & Morano, K. A. (2005) · Genetics · doi:10.1534/genetics.105.043109 · Cited by 55
Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway
Oh, J., Hyun, J.-Y., & Varshavsky, A. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705898114 · Cited by 55
The yeast heat shock response is induced by conversion of cells to spheroplasts and by potent transcriptional inhibitors
Adams, C. C., & Gross, D. S. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.23.7429-7435.1991 · Cited by 55
Hsp90 Chaperone Activity Requires the Full-length Protein and Interaction among Its Multiple Domains
Johnson, B. D., Chadli, A., Felts, S. J., Bouhouche, I., CATELLI, M. G., & Toft, D. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005195200 · Cited by 55
Functions of the Hsp90 chaperone system: lifting client proteins to new heights.
Eckl, J. M., & Richter, K. (2013) · Europe PMC (PubMed Central) · Cited by 53
Sequencing and De Novo Assembly of the Western Tarnished Plant Bug (Lygus hesperus) Transcriptome
Hull, J. J., Geib, S. M., Fabrick, J. A., & Brent, C. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055105 · Cited by 54
Intracellular localization of the 90 kDA heat shock protein (HSP90α) determined by expression of a EGFP—HSP90α‐fusion protein in unstressed and heat stressed 3T3 cells
Langer, T., Rosmus, S., & Fasold, H. (2003) · Cell Biology International · doi:10.1016/s1065-6995(02)00256-1 · Cited by 54
Heat Shock Protein 90: A Unique Chemotherapeutic Target
Cullinan, S. B., & Whitesell, L. J. (2006) · Seminars in Oncology · doi:10.1053/j.seminoncol.2006.04.001 · Cited by 55
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Pagant, S., Kung, L., Dorrington, M., Lee, M., & Miller, E. A. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0046 · Cited by 54
Heat-induced Oligomerization of the Molecular Chaperone Hsp90
Chadli, A., Ladjimi, M. M., Baulieu, É.-É., & CATELLI, M. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4133 · Cited by 53
A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication
Zarzov, P., Boucherie, H., & Mann, C. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.16.1879 · Cited by 53
Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90β, a property that can be exploited in screens for new Hsp90 chaperone inhibitors
Piper, P. W., Panaretou, B., Millson, S. H., Trumana, A., Mollapour, M., Pearl, L. H., & Prodromou, C. (2003) · Gene · doi:10.1016/s0378-1119(02)01102-2 · Cited by 53
A comparison of Hsp90α and Hsp90β interactions with cochaperones and substrates
Taherian, A., Krone, P. H., & Ovsenek, N. (2008) · Biochemistry and Cell Biology · doi:10.1139/o07-154 · Cited by 52
Cns1 Is an Activator of the Ssa1 ATPase Activity
Hainzl, O., Wegele, H., Richter, K., & Büchner, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402189200 · Cited by 51
The Peptidyl-prolyl Isomerase Domain of the CyP-40 Cyclophilin Homolog Cpr7 Is Not Required to Support Growth or Glucocorticoid Receptor Activity in Saccharomyces cerevisiae
Duina, A. A., Marsh, J. A., Kurtz, R. B., Chang, H.-C. J., Lindquist, S. L., & Gaber, R. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.10819 · Cited by 51
Self-citation
Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae
Kimura, Y., Matsumoto, S., & Yahara, I. (1994) · Molecular and General Genetics MGG · doi:10.1007/bf00285275 · Cited by 51
Hsp90: From Cellular to Organismal Proteostasis
Somogyvári, M., Khatatneh, S., & Sőti, C. (2022) · Cells · doi:10.3390/cells11162479 · Cited by 55
Functional Interactions between Hsp90 and the Co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae
Tesic, M., Marsh, J. A., Cullinan, S. B., & Gaber, R. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304315200 · Cited by 50
Heat Shock Factor Gains Access to the Yeast HSC82 Promoter Independently of Other Sequence-Specific Factors and Antagonizes Nucleosomal Repression of Basal and Induced Transcription
Erkine, A. M., Adams, C. C., Diken, T., & Gross, D. S. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.7004 · Cited by 50
Hsp90 and its co‐chaperone Sti1 control TDP‐43 misfolding and toxicity
Lin, L. T., Razzaq, A., Gregorio, S. E. D., Hong, S., Charles, B., Lopes, M. H., Beraldo, F. H., Prado, V. F., Prado, M. A. M., & Duennwald, M. L. (2021) · The FASEB Journal · doi:10.1096/fj.202002645r · Cited by 51
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The decline of porcine sperm motility by geldanamycin, a specific inhibitor of heat-shock protein 90 (hsp90)
Huang, S., Kuo, Y. H., Tsou, H. L., Lee, Y. P., King, Y., Huang, H. C., Yang, P. C., & Lee, W. C. (2000) · Theriogenology · doi:10.1016/s0093-691x(00)00262-4 · Cited by 49
HtpG is involved in the pathogenesis of Edwardsiella tarda
Dang, W., Hu, Y., & Sun, L. (2011) · Veterinary Microbiology · doi:10.1016/j.vetmic.2011.05.030 · Cited by 49
Tyrosine nitration as mediator of cell death
Franco, M. C., & Estévez, Á. G. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1662-8 · Cited by 50
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Authors: Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Borkovich, K A
Finkelstein, D B
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1989-09
Volume: 9
Issue: 9
Pages: 3919-3930
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.9.9.3919
PMC: PMC362454
OpenAlex: W1956379070
Cited by: 641
References: 54
Citations by year: 2026: 1 · 2025: 5 · 2024: 22 · 2023: 11 · 2022: 19 · 2021: 16 · 2020: 15 · 2019: 23 · 2018: 16 · 2017: 16 · 2016: 18 · 2015: 11 · 2014: 32 · 2013: 26 · 2012: 24
FWCI: 5.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (GM 11223, GM3582, GM25829)
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 › Ubiquitin and proteasome pathways
Keywords: Hsp82, heat shock proteins, Saccharomyces cerevisiae, heat tolerance, gene copy number, site-directed mutagenesis, protein-protein complex formation, molecular chaperones, constitutive expression
MeSH terms: Amino Acid Sequence, Base Sequence, DNA, Fungal, Gene Expression Regulation, Genes, Fungal, Multigene Family, Hot Temperature, Heat-Shock Proteins, Molecular Sequence Data, Mutation, Saccharomyces cerevisiae, Spores, Fungal

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hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

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