HSP82

Summary

Gene Symbol: HSP82
Description: Hsp90 family chaperone HSP82
Alias: HSP90, Hsp90 family chaperone HSP82
Species: Saccharomyces cerevisiae S288c
Products:     HSP82

Top Publications

  1. Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan J, Singh S, et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell. 2002;10:1307-18 pubmed
    Client protein activation by Hsp90 involves a plethora of cochaperones whose roles are poorly defined...
  2. Obermann W, Sondermann H, Russo A, Pavletich N, Hartl F. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol. 1998;143:901-10 pubmed
    Heat shock protein 90 (Hsp90), an abundant molecular chaperone in the eukaryotic cytosol, is involved in the folding of a set of cell regulatory proteins and in the re-folding of stress-denatured polypeptides...
  3. Staresincic L, Walker J, Dirac Svejstrup A, Mitter R, Svejstrup J. GTP-dependent binding and nuclear transport of RNA polymerase II by Npa3 protein. J Biol Chem. 2011;286:35553-61 pubmed publisher
    ..Together, our data suggest that Npa3 defines an unconventional pathway for nuclear import of RNAPII, which involves GTP-dependent binding of Npa3 to the polymerase. ..
  4. Richter K, Walter S, Buchner J. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J Mol Biol. 2004;342:1403-13 pubmed
    The molecular chaperone Hsp90 mediates the ATP-dependent activation of a large number of proteins involved in signal transduction...
  5. Siligardi G, Panaretou B, Meyer P, Singh S, Woolfson D, Piper P, et al. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. J Biol Chem. 2002;277:20151-9 pubmed
    In vivo activation of client proteins by Hsp90 depends on its ATPase-coupled conformational cycle and on interaction with a variety of co-chaperone proteins...
  6. Wayne N, Bolon D. Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers. J Biol Chem. 2007;282:35386-95 pubmed
    Heat shock protein 90 (Hsp90) plays a central role in signal transduction and has emerged as a promising target for anti-cancer therapeutics, but its molecular mechanism is poorly understood...
  7. Morano K, Santoro N, Koch K, Thiele D. A trans-activation domain in yeast heat shock transcription factor is essential for cell cycle progression during stress. Mol Cell Biol. 1999;19:402-11 pubmed
    ..When expressed at physiological levels in HSF(1-583) cells, the inducible Hsp90 isoform encoded by HSP82 more efficiently suppressed the temperature sensitivity of this strain than the constitutively expressed gene ..
  8. Prodromou C, Siligardi G, O Brien R, Woolfson D, Regan L, Panaretou B, et al. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J. 1999;18:754-62 pubmed
    The in vivo function of the heat shock protein 90 (Hsp90) molecular chaperone is dependent on the binding and hydrolysis of ATP, and on interactions with a variety of co-chaperones containing tetratricopeptide repeat (TPR) domains...
  9. Toogun O, Dezwaan D, Freeman B. The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol. 2008;28:457-67 pubmed
    The Hsp90 molecular chaperone is a highly abundant eukaryotic molecular chaperone...

More Information

Publications80

  1. Borkovich K, Farrelly F, Finkelstein D, Taulien J, Lindquist S. hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol. 1989;9:3919-30 pubmed
    b>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...
  2. Pursell N, Mishra P, Bolon D. Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth. Eukaryot Cell. 2012;11:1033-41 pubmed publisher
    The Hsp90 chaperone is required for the maturation of signal transduction clients, including many kinases and nuclear steroid hormone receptors...
  3. Richter K, Moser S, Hagn F, Friedrich R, Hainzl O, Heller M, et al. Intrinsic inhibition of the Hsp90 ATPase activity. J Biol Chem. 2006;281:11301-11 pubmed
    The molecular chaperone Hsp90 is required for the folding and activation of a large number of substrate proteins. These are involved in essential cellular processes ranging from signal transduction to viral replication...
  4. Nathan D, Vos M, Lindquist S. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci U S A. 1997;94:12949-56 pubmed
    ..In vivo, Hsp90 (heat shock protein 90) plays a role in the maturation of components of signal transduction pathways but also ..
  5. Mollapour M, Tsutsumi S, Truman A, Xu W, Vaughan C, Beebe K, et al. Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell. 2011;41:672-81 pubmed publisher
    Heat shock protein 90 (Hsp90) is an essential molecular chaperone whose activity is regulated not only by cochaperones but also by distinct posttranslational modifications...
  6. Millson S, Vaughan C, Zhai C, Ali M, Panaretou B, Piper P, et al. Chaperone ligand-discrimination by the TPR-domain protein Tah1. Biochem J. 2008;413:261-8 pubmed publisher
    ..involved in protein-protein interactions and a number have been characterized that interact either with Hsp70 or Hsp90, but a few can bind both chaperones...
  7. Flom G, Weekes J, Williams J, Johnson J. Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae. Genetics. 2006;172:41-51 pubmed
    Through simultaneous interactions with Hsp70 and Hsp90 via separate tetratricopeptide repeat (TPR) domains, the cochaperone protein Hop/Sti1 has been proposed to play a critical role in the transfer of client proteins from Hsp70 to Hsp90...
  8. Chang H, Nathan D, Lindquist S. In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol Cell Biol. 1997;17:318-25 pubmed
    b>Hsp90 interacts with Sti1 (p60) in lysates of yeast and vertebrate cells. Here we provide the first analysis of their interaction in vivo...
  9. Eckert K, Saliou J, Monlezun L, Vigouroux A, Atmane N, Caillat C, et al. The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity. J Biol Chem. 2010;285:31304-12 pubmed publisher
    b>Hsp90 (heat shock protein 90) is an ATP-dependent molecular chaperone regulated by collaborating proteins called cochaperones...
  10. Imai J, Yahara I. Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin. Mol Cell Biol. 2000;20:9262-70 pubmed
    The role of HSP90 in stress tolerance was investigated in Saccharomyces cerevisiae. Cells showing 20-fold overexpression of Hsc82, an HSP90 homologue in yeast, were hypersensitive to high-NaCl or H-LiCl stresses...
  11. Flom G, Lemieszek M, Fortunato E, Johnson J. Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins. Mol Biol Cell. 2008;19:5249-58 pubmed publisher
    ..Hsp70 of the Ssa family in the translocation of preproteins to the ER and mitochondria and in the maturation of Hsp90 client proteins...
  12. Fang Y, Fliss A, Rao J, Caplan A. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol Cell Biol. 1998;18:3727-34 pubmed
    ..by PCR amplification from yeast genomic DNA following its identification as encoding an ortholog of human p23, an Hsp90 cochaperone...
  13. Wegele H, Haslbeck M, Reinstein J, Buchner J. Sti1 is a novel activator of the Ssa proteins. J Biol Chem. 2003;278:25970-6 pubmed
    The molecular chaperones Hsp70 and Hsp90 are involved in the folding and maturation of key regulatory proteins in eukaryotes...
  14. Nakatsukasa K, Huyer G, Michaelis S, Brodsky J. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell. 2008;132:101-12 pubmed publisher
    ..These data indicate that polytopic membrane proteins can be extracted from the ER, and define the point of action of chaperones and the requirement for Ufd2p during membrane protein quality control...
  15. Yang X, Maurer K, Molanus M, Mager W, Siderius M, van der Vies S. The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae. FEMS Yeast Res. 2006;6:195-204 pubmed
    ..Rather, the hsp82 mutants display features that are characteristic for cell-wall mutants, i.e...
  16. Meyer P, Prodromou C, Liao C, Hu B, Roe S, Vaughan C, et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 2004;23:1402-10 pubmed
    b>Hsp90 is a molecular chaperone essential for the activation and assembly of many key eukaryotic signalling and regulatory proteins...
  17. Prodromou C, Roe S, Piper P, Pearl L. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nat Struct Biol. 1997;4:477-82 pubmed
    b>Hsp90 is a highly specific chaperone for many signal transduction proteins, including steroid hormone receptors and a broad range of protein kinases...
  18. Chang H, Lindquist S. Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae. J Biol Chem. 1994;269:24983-8 pubmed
    ..We utilized affinity chromatography to investigate whether Hsp82, the Hsp90 of Saccharomyces cerevisiae, is found in similar complexes in that organism...
  19. Mollapour M, Tsutsumi S, Donnelly A, Beebe K, Tokita M, Lee M, et al. Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function. Mol Cell. 2010;37:333-43 pubmed publisher
    Saccharomyces WEE1 (Swe1), the only "true" tyrosine kinase in budding yeast, is an Hsp90 client protein...
  20. Ali M, Roe S, Vaughan C, Meyer P, Panaretou B, Piper P, et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature. 2006;440:1013-7 pubmed
    b>Hsp90 (heat shock protein of 90 kDa) is a ubiquitous molecular chaperone responsible for the assembly and regulation of many eukaryotic signalling systems and is an emerging target for rational chemotherapy of many cancers...
  21. Abbas Terki T, Donze O, Briand P, Picard D. Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol Cell Biol. 2001;21:7569-75 pubmed
    The highly abundant molecular chaperone Hsp90 functions with assistance from auxiliary factors, collectively referred to as Hsp90 cochaperones, and the Hsp70 system...
  22. Siligardi G, Hu B, Panaretou B, Piper P, Pearl L, Prodromou C. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J Biol Chem. 2004;279:51989-98 pubmed
    ATP hydrolysis by the Hsp90 molecular chaperone requires a connected set of conformational switches triggered by ATP binding to the N-terminal domain in the Hsp90 dimer...
  23. Jarosz D, Lindquist S. Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science. 2010;330:1820-4 pubmed publisher
    ..undergo rapid diversification? By linking genetic variation to phenotypic variation via environmental stress, the Hsp90 protein-folding reservoir might promote both stasis and change...
  24. Nathan D, Vos M, Lindquist S. Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc Natl Acad Sci U S A. 1999;96:1409-14 pubmed
    b>Hsp90 functions in a multicomponent chaperone system to promote the maturation and maintenance of a diverse, but specific, set of target proteins that play key roles in the regulation of cell growth and development...
  25. Lotz G, Lin H, Harst A, Obermann W. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem. 2003;278:17228-35 pubmed
    The ATP-dependent molecular chaperone Hsp90 is an essential and abundant stress protein in the eukaryotic cytosol that cooperates with a cohort of cofactors/cochaperones to fulfill its cellular tasks...
  26. Lee P, Shabbir A, Cardozo C, Caplan A. Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Mol Biol Cell. 2004;15:1785-92 pubmed
    b>Hsp90 functions in association with several cochaperones for folding of protein kinases and transcription factors, although the relative contribution of each to the overall reaction is unknown...
  27. Flom G, Weekes J, Johnson J. Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae. Curr Genet. 2005;47:368-80 pubmed
    b>Hsp90 is an essential molecular chaperone that is critical for the activity of diverse cellular proteins. Hsp90 functions with a number of co-chaperone proteins, including Sti1/Hop...
  28. Cowen L, Lindquist S. Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science. 2005;309:2185-9 pubmed
    b>Hsp90 is a molecular chaperone for many signal transducers and may influence evolution by releasing previously silent genetic variation in response to environmental change...
  29. Liu X, Morano K, Thiele D. The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. J Biol Chem. 1999;274:26654-60 pubmed
    ..The HSC82 and HSP82 genes, encoding isoforms of the yeast Hsp90 molecular chaperone, were recently identified as targets of the HSF carboxyl-terminal activation domain (CTA), ..
  30. Back R, Dominguez C, Rothé B, Bobo C, Beaufils C, Morera S, et al. High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex. Structure. 2013;21:1834-47 pubmed publisher
    The ubiquitous Hsp90 chaperone participates in snoRNP and RNA polymerase assembly through interaction with the R2TP complex. This complex includes the proteins Tah1, Pih1, Rvb1, and Rvb2. Tah1 bridges Hsp90 to R2TP...
  31. Millson S, Nuttall J, Mollapour M, Piper P. The Hsp90/Cdc37p chaperone system is a determinant of molybdate resistance in Saccharomyces cerevisiae. Yeast. 2009;26:339-47 pubmed publisher
    ..Instead, high molybdate levels are inhibitory to its growth. Low cellular levels of heat shock protein 90 (Hsp90), an essential chaperone, were found to enhance this sensitivity to molybdate...
  32. Hoffman K, Duennwald M, Karagiannis J, Genereaux J, McCarton A, Brandl C. Saccharomyces cerevisiae Tti2 Regulates PIKK Proteins and Stress Response. G3 (Bethesda). 2016;6:1649-59 pubmed publisher
    ..We also find that overexpressing Hsp90 or its cochaperones is synthetic lethal when Tti2 is depleted, an effect possibly due to imbalanced stoichiometry ..
  33. Song H, Fan P, Shi W, Zhao R, Li Y. Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals functional differences of AtHsp90s under abiotic stresses. J Plant Physiol. 2010;167:1172-8 pubmed publisher
    The genome of Arabidopsis thaliana contains seven Hsp90 family genes...
  34. Armstrong H, Wolmarans A, Mercier R, Mai B, LaPointe P. The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922. PLoS ONE. 2012;7:e49322 pubmed publisher
    b>Hsp90 is a dimeric ATPase responsible for the activation or maturation of a specific set of substrate proteins termed 'clients'...
  35. Jiang L, Mishra P, Hietpas R, Zeldovich K, Bolon D. Latent effects of Hsp90 mutants revealed at reduced expression levels. PLoS Genet. 2013;9:e1003600 pubmed publisher
    ..systematically investigated the fitness effects of point mutations in a putative substrate binding loop of yeast Hsp90 (Hsp82) over a broad range of expression strengths...
  36. Johnson J, Zuehlke A, Tenge V, Langworthy J. Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones. Curr Genet. 2014;60:265-76 pubmed publisher
    The essential molecular chaperone Hsp90 functions with over ten co-chaperones in Saccharomyces cerevisiae, but the in vivo roles of many of these co-chaperones are poorly understood...
  37. Bandhakavi S, McCann R, Hanna D, Glover C. A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases. J Biol Chem. 2003;278:2829-36 pubmed
    We report here the identification of CDC37, which encodes a putative Hsp90 co-chaperone, as a multicopy suppressor of a temperature-sensitive allele (cka2-13(ts)) of the CKA2 gene encoding the alpha' catalytic subunit of protein kinase ..
  38. Wandinger S, Suhre M, Wegele H, Buchner J. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J. 2006;25:367-76 pubmed
    ..Ppt1 is known to bind to Hsp90, a molecular chaperone that performs essential functions in the folding and activation of a large number of client ..
  39. Dezwaan D, Toogun O, Echtenkamp F, Freeman B. The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states. Nat Struct Mol Biol. 2009;16:711-6 pubmed publisher
    ..Notably, the yeast Hsp90 chaperone Hsp82 mediates the switch between the telomere capping and extending structures by modulating the DNA binding activity ..
  40. Dutton B, Kitson R, Parry Morris S, Roe S, Prodromou C, Moody C. Synthesis of macrolactam analogues of radicicol and their binding to heat shock protein Hsp90. Org Biomol Chem. 2014;12:1328-40 pubmed publisher
    ..Final deprotection of the phenolic groups gives the desired macrolactams whose binding to the N-terminal domain of yeast Hsp90 was studied by isothermal titration calorimetry and protein X-ray crystallography.
  41. Meyer P, Prodromou C, Hu B, Vaughan C, Roe S, Panaretou B, et al. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol Cell. 2003;11:647-58 pubmed
    Activation of client proteins by the Hsp90 molecular chaperone is dependent on binding and hydrolysis of ATP, which drives a molecular clamp via transient dimerization of the N-terminal domains...
  42. Finnigan G, Duvalyan A, Liao E, Sargsyan A, Thorner J. Detection of protein-protein interactions at the septin collar in Saccharomyces cerevisiae using a tripartite split-GFP system. Mol Biol Cell. 2016;27:2708-25 pubmed publisher
    ..even with highly abundant cytosolic proteins readily accessible to the bud neck (including molecular chaperone Hsp82 and glycolytic enzyme Pgk1)...
  43. Bansal P, Abdulle R, Kitagawa K. Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex. Mol Cell Biol. 2004;24:8069-79 pubmed
    ..Formation of the active Ctf13-Skp1 complex also requires Hsp90, a molecular chaperone. We have found that Sgt1 interacts with Hsp90 in yeast...
  44. Lee H, Hon T, Lan C, Zhang L. Structural environment dictates the biological significance of heme-responsive motifs and the role of Hsp90 in the activation of the heme activator protein Hap1. Mol Cell Biol. 2003;23:5857-66 pubmed
    ..diminished the extent of Hap1 activation by heme and moderately enhanced the interaction of Hap1 with Hsp90. Furthermore, deletions of nonregulatory sequences completely abolished heme activation of Hap1 and greatly ..
  45. Geymonat M, Wang L, Garreau H, Jacquet M. Ssa1p chaperone interacts with the guanine nucleotide exchange factor of ras Cdc25p and controls the cAMP pathway in Saccharomyces cerevisiae. Mol Microbiol. 1998;30:855-64 pubmed
    ..b>Hsp82 appeared also to be co-immunoprecipitated with Cdc25p, albeit to a lower level than Hsp70...
  46. Mickler M, Hessling M, Ratzke C, Buchner J, Hugel T. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat Struct Mol Biol. 2009;16:281-6 pubmed publisher
    The molecular chaperone heat-shock protein 90 (Hsp90) is one of the most abundant proteins in unstressed eukaryotic cells. Its function is dependent on an exceptionally slow ATPase reaction that involves large conformational changes...
  47. Young J, Hoogenraad N, Hartl F. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell. 2003;112:41-50 pubmed
    ..Here, we show that in mammals, the cytosolic chaperones Hsp90 and Hsp70 dock onto a specialized TPR domain in the import receptor Tom70 at the outer mitochondrial membrane...
  48. Donze O, Picard D. Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]. Mol Cell Biol. 1999;19:8422-32 pubmed
    ..Using genetic and biochemical approaches, we show that Gcn2 is regulated by the molecular chaperone Hsp90 in budding yeast Saccharomyces cerevisiae...
  49. Röhl A, Wengler D, Madl T, Lagleder S, Tippel F, Herrmann M, et al. Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules. Nat Commun. 2015;6:6655 pubmed publisher
    The cochaperone Sti1/Hop physically links Hsp70 and Hsp90. The protein exhibits one binding site for Hsp90 (TPR2A) and two binding sites for Hsp70 (TPR1 and TPR2B). How these sites are used remained enigmatic...
  50. Qiu Y, Ge Q, Wang M, Lv H, Ebrahimi M, Niu L, et al. The crystal structure of the Hsp90 co-chaperone Cpr7 from Saccharomyces cerevisiae. J Struct Biol. 2017;197:379-387 pubmed publisher
    The versatility of Hsp90 can be attributed to the variety of co-chaperone proteins that modulate the role of Hsp90 in many cellular processes...
  51. Buttner S, Ruli D, Vögtle F, Galluzzi L, Moitzi B, Eisenberg T, et al. A yeast BH3-only protein mediates the mitochondrial pathway of apoptosis. EMBO J. 2011;30:2779-92 pubmed publisher
    ..Thus, the yeast genome encodes a functional BH3 domain that induces cell death through phylogenetically conserved mechanisms. ..
  52. Sahasrabudhe P, Rohrberg J, Biebl M, Rutz D, Buchner J. The Plasticity of the Hsp90 Co-chaperone System. Mol Cell. 2017;67:947-961.e5 pubmed publisher
    The Hsp90 system in the eukaryotic cytosol is characterized by a cohort of co-chaperones that bind to Hsp90 and affect its function...
  53. Li J, Richter K, Buchner J. Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol. 2011;18:61-6 pubmed publisher
    The chaperone cycle of heat shock protein-90 (Hsp90) involves progression through defined complexes with different cochaperones. It is still enigmatic how the exchange of cochaperones is regulated...
  54. Imai J, Maruya M, Yashiroda H, Yahara I, Tanaka K. The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 2003;22:3557-67 pubmed
    b>Hsp90 has a diverse array of cellular roles including protein folding, stress response and signal transduction. Herein we report a novel function for Hsp90 in the ATP-dependent assembly of the 26S proteasome...
  55. Singh H, Erkine A, Kremer S, Duttweiler H, Davis D, Iqbal J, et al. A functional module of yeast mediator that governs the dynamic range of heat-shock gene expression. Genetics. 2006;172:2169-84 pubmed
    ..In an effort to identify these factors, we isolated spontaneous extragenic suppressors of hsp82-deltaHSE1, an allele of HSP82 that bears a 32-bp deletion of its high-affinity HSF-binding site, yet retains its ..
  56. Lee H, Hon T, Zhang L. The molecular chaperone Hsp90 mediates heme activation of the yeast transcriptional activator Hap1. J Biol Chem. 2002;277:7430-7 pubmed
    b>Hsp90 plays critical roles in the proper functioning of a wide array of eukaryotic signal transducers such as steroid receptors and tyrosine kinases. Hap1 is a naturally occurring substrate of Hsp90 in Saccharomyces cerevisiae...
  57. Villanyi Z, Ribaud V, Kassem S, Panasenko O, Pahi Z, Gupta I, et al. The Not5 subunit of the ccr4-not complex connects transcription and translation. PLoS Genet. 2014;10:e1004569 pubmed publisher
    ..This stems from the importance of Not5 for the association of the R2TP Hsp90 co-chaperone with polysomes translating RPB1 mRNA to protect newly synthesized Rpb1 from aggregation...
  58. Johnson R, Prakash L, Prakash S. Pol31 and Pol32 subunits of yeast DNA polymerase ? are also essential subunits of DNA polymerase ?. Proc Natl Acad Sci U S A. 2012;109:12455-60 pubmed publisher
    ..To distinguish the four-subunit complex from the two-subunit Pol?, we designate the four-subunit enzyme "Pol?-d," where "-d" denotes the Pol31/Pol32 subunits of Pol?. ..
  59. Reidy M, Masison D. Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104. Mol Cell Biol. 2010;30:3542-52 pubmed publisher
    ..repeat (TPR) interaction motif was dispensable for curing; however, cells expressing Sti1 defective in Hsp70 or Hsp90 interaction cured less efficiently, and the Hsp90 inhibitor radicicol abolished curing, implying that Sti1 acts in ..
  60. Lorenz O, Freiburger L, Rutz D, Krause M, Zierer B, Alvira S, et al. Modulation of the Hsp90 chaperone cycle by a stringent client protein. Mol Cell. 2014;53:941-53 pubmed publisher
    b>Hsp90 is the most abundant molecular chaperone in the eukaryotic cell. One of the most stringent clients is the glucocorticoid receptor (GR), whose in vivo function strictly depends on the interaction with the Hsp90 machinery...
  61. Tapia H, Morano K. Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast. Mol Biol Cell. 2010;21:63-72 pubmed publisher
    ..Hsp90 nuclear accumulation was unaffected in sba1Delta cells, demonstrating that Hsp82 translocates independently of Sba1...
  62. Abbas Terki T, Donze O, Picard D. The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest. FEBS Lett. 2000;467:111-6 pubmed
    The molecular chaperone Cdc37 is thought to act in part as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex. We demonstrate here that Cdc37 is required for activity of the kinase Ste11 in budding yeast...
  63. Scheibel T, Weikl T, Rimerman R, Smith D, Lindquist S, Buchner J. Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae. Mol Microbiol. 1999;34:701-13 pubmed
    The molecular chaperone Hsp90 is a regulatory component of some key signalling proteins in the cytosol of eukaryotic cells. For some of these functions, its interaction with co-chaperones is required...
  64. Rødkær S, Pultz D, Brusch M, Bennetzen M, Falkenby L, Andersen J, et al. Quantitative proteomics identifies unanticipated regulators of nitrogen- and glucose starvation. Mol Biosyst. 2014;10:2176-88 pubmed publisher
    ..identified the cyclin-dependent kinase (CDK) inhibitor Sic1, the Hsp90 co-chaperone Cdc37, and the Hsp90 isoform Hsp82 to putatively mediate some of the starvation responses...
  65. Mollapour M, Bourboulia D, Beebe K, Woodford M, Polier S, Hoang A, et al. Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors. Mol Cell. 2014;53:317-29 pubmed publisher
    ..proteins in both normal and cancer cells depends on the dimeric molecular chaperone heat shock protein 90 (Hsp90)...
  66. Laskar S, K S, Bhattacharyya M, Nair A, Dhar P, Bhattacharyya S. Heat stress-induced Cup9-dependent transcriptional regulation of SIR2. Mol Cell Biol. 2015;35:437-50 pubmed publisher
    ..b>Hsp82 overexpression, which is the usual outcome of heat shock treatment, leads to a similar downregulation of SIR2 ..
  67. Hessling M, Richter K, Buchner J. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat Struct Mol Biol. 2009;16:287-93 pubmed publisher
    The molecular chaperone heat-shock protein 90 (Hsp90) couples ATP hydrolysis to conformational changes driving a reaction cycle that is required for substrate activation...
  68. Li J, Qian X, Hu J, Sha B. Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading. J Biol Chem. 2009;284:23852-9 pubmed publisher
    ..The preproteins are escorted to Tom70/Tom71 by molecular chaperones Hsp70 and Hsp90. Here we present the high resolution crystal structures of Tom71 and the protein complexes between Tom71 and the ..
  69. Basmaji F, Martin Yken H, Durand F, Dagkessamanskaia A, Pichereaux C, Rossignol M, et al. The 'interactome' of the Knr4/Smi1, a protein implicated in coordinating cell wall synthesis with bud emergence in Saccharomyces cerevisiae. Mol Genet Genomics. 2006;275:217-30 pubmed
  70. Naticchia M, Brown H, Garcia F, Lamade A, Justice S, Herrin R, et al. Bifunctional electrophiles cross-link thioredoxins with redox relay partners in cells. Chem Res Toxicol. 2013;26:490-7 pubmed publisher
    ..Taken together, our results indicate that bifunctional electrophiles potentially disrupt redox homeostasis in yeast and human cells by forming cross-linked complexes between thioredoxins and their redox partners. ..
  71. Mandal A, Gibney P, Nillegoda N, Theodoraki M, Caplan A, Morano K. Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol Cell. 2010;21:1439-48 pubmed publisher
    ..a central role in protein homeostasis and quality control in conjunction with other chaperone machines, including Hsp90. The Hsp110 chaperone Sse1 promotes Hsp90 activity in yeast, and functions as a nucleotide exchange factor (NEF) ..