[1]
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NUCLEOTIDE SEQUENCE.
PubMed=6325446 [NCBI, ExPASy, EBI, Israel, Japan]
Farrelly F.W.,
Finkelstein D.B.;
"Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae.";
J. Biol. Chem. 259:5745-5751(1984).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H.,
Storms R.K.,
Ahmed A.,
Albermann K.,
Allen E.,
Ansorge W.,
Araujo R.,
Aparicio A.,
Barrell B.G.,
Badcock K.,
Benes V.,
Botstein D.,
Bowman S.,
Brueckner M.,
Carpenter J.,
Cherry J.M.,
Chung E.,
Churcher C.M.,
Coster F., ![]()
Davis K.,
Davis R.W.,
Dietrich F.S.,
Delius H.,
DiPaolo T.,
Dubois E.,
Duesterhoeft A.,
Duncan M.,
Floeth M.,
Fortin N.,
Friesen J.D.,
Fritz C.,
Goffeau A.,
Hall J.,
Hebling U.,
Heumann K.,
Hilbert H.,
Hillier L.W.,
Hunicke-Smith S.,
Hyman R.W.,
Johnston M.,
Kalman S.,
Kleine K.,
Komp C.,
Kurdi O.,
Lashkari D.,
Lew H.,
Lin A.,
Lin D.,
Louis E.J.,
Marathe R.,
Messenguy F.,
Mewes H.-W.,
Mirtipati S.,
Moestl D.,
Mueller-Auer S.,
Namath A.,
Nentwich U.,
Oefner P.,
Pearson D.,
Petel F.X.,
Pohl T.M.,
Purnelle B.,
Rajandream M.A.,
Rechmann S.,
Rieger M.,
Riles L.,
Roberts D.,
Schaefer M.,
Scharfe M.,
Scherens B.,
Schramm S.,
Schroeder M.,
Sdicu A.-M.,
Tettelin H.,
Urrestarazu L.A.,
Ushinsky S.,
Vierendeels F.,
Vissers S.,
Voss H.,
Walsh S.V.,
Wambutt R.,
Wang Y.,
Wedler E.,
Wedler H.,
Winnett E.,
Zhong W.-W.,
Zollner A.,
Vo D.H.,
Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
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[3]
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INDUCTION.
PubMed=2674684 [NCBI, ExPASy, EBI, Israel, Japan]
Borkovich K.A.,
Farrelly F.W.,
Finkelstein D.B.,
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. 9:3919-3930(1989).
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[4]
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ATPASE ACTIVITY.
PubMed=8419347 [NCBI, ExPASy, EBI, Israel, Japan]
Nadeau K.,
Das A.,
Walsh C.T.;
"Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases.";
J. Biol. Chem. 268:1479-1487(1993).
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[5]
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MUTAGENESIS OF GLY-313; GLU-431; THR-525; ALA-576 AND ARG-579.
PubMed=8248264 [NCBI, ExPASy, EBI, Israel, Japan]
Bohen S.P.,
Yamamoto K.R.;
"Isolation of Hsp90 mutants by screening for decreased steroid receptor function.";
Proc. Natl. Acad. Sci. U.S.A. 90:11424-11428(1993).
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[6]
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INTERACTION WITH STI1 AND CPR6.
PubMed=7929182 [NCBI, ExPASy, EBI, Israel, Japan]
Chang H.-C.J.,
Lindquist S.;
"Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae.";
J. Biol. Chem. 269:24983-24988(1994).
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[7]
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MUTAGENESIS OF THR-22; ALA-41; GLY-81; THR-101; GLY-170; GLY-313; GLU-381 AND ALA-587.
PubMed=7791797 [NCBI, ExPASy, EBI, Israel, Japan]
Nathan D.F.,
Lindquist S.;
"Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.";
Mol. Cell. Biol. 15:3917-3925(1995).
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[8]
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INTERACTION WITH CPR6 AND CPR7.
DOI=10.1126/science.274.5293.1713; PubMed=8939862 [NCBI, ExPASy, EBI, Israel, Japan]
Duina A.A.,
Chang H.-C.J.,
Marsh J.A.,
Lindquist S.,
Gaber R.F.;
"A cyclophilin function in Hsp90-dependent signal transduction.";
Science 274:1713-1715(1996).
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[9]
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INDUCTION.
PubMed=9296388 [NCBI, ExPASy, EBI, Israel, Japan]
Zarzov P.,
Boucherie H.,
Mann C.;
"A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication.";
J. Cell Sci. 110:1879-1891(1997).
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[10]
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INTERACTION WITH SBA1, AND MUTAGENESIS OF ALA-97 AND SER-485.
PubMed=9632755 [NCBI, ExPASy, EBI, Israel, Japan]
Fang Y.,
Fliss A.E.,
Rao J.,
Caplan A.J.;
"SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins.";
Mol. Cell. Biol. 18:3727-3734(1998).
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[11]
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INTERACTION WITH HAP1.
PubMed=9632766 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang L.,
Hach A.,
Wang C.;
"Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1.";
Mol. Cell. Biol. 18:3819-3828(1998).
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[12]
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INTERACTION WITH CNS1.
PubMed=9819421 [NCBI, ExPASy, EBI, Israel, Japan]
Dolinski K.J.,
Cardenas M.E.,
Heitman J.;
"CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90.";
Mol. Cell. Biol. 18:7344-7352(1998).
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[13]
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INTERACTION WITH SSE1.
DOI=10.1074/jbc.274.38.26654; PubMed=10480867 [NCBI, ExPASy, EBI, Israel, Japan]
Liu X.-D.,
Morano K.A.,
Thiele D.J.;
"The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.";
J. Biol. Chem. 274:26654-26660(1999).
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[14]
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INTERACTION WITH GCN2.
PubMed=10567567 [NCBI, ExPASy, EBI, Israel, Japan]
Donze O.,
Picard D.;
"Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2.";
Mol. Cell. Biol. 19:8422-8432(1999).
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[15]
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BINDING TO TPR REPEATS.
DOI=10.1016/S0092-8674(00)80830-2; PubMed=10786835 [NCBI, ExPASy, EBI, Israel, Japan]
Scheufler C.,
Brinker A.,
Bourenkov G.,
Pegoraro S.,
Moroder L.,
Bartunik H.,
Hartl F.U.,
Moarefi I.;
"Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.";
Cell 101:199-210(2000).
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[16]
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ATPASE ACTIVITY, AND MUTAGENESIS OF ALA-107.
DOI=10.1093/emboj/19.16.4383; PubMed=10944121 [NCBI, ExPASy, EBI, Israel, Japan]
Prodromou C.,
Panaretou B.,
Chohan S.,
Siligardi G.,
O'Brien R.,
Ladbury J.E.,
Roe S.M.,
Piper P.W.,
Pearl L.H.;
"The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains.";
EMBO J. 19:4383-4392(2000).
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[17]
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INTERACTION WITH CDC37 AND STE11.
DOI=10.1016/S0014-5793(00)01134-0; PubMed=10664467 [NCBI, ExPASy, EBI, Israel, Japan]
Abbas-Terki T.,
Donze O.,
Picard D.;
"The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest.";
FEBS Lett. 467:111-116(2000).
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[18]
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INTERACTION WITH AHA1 AND HCH1.
DOI=10.1016/S1097-2765(02)00785-2; PubMed=12504007 [NCBI, ExPASy, EBI, Israel, Japan]
Panaretou B.,
Siligardi G.,
Meyer P.,
Maloney A.,
Sullivan J.K.,
Singh S.,
Millson S.H.,
Clarke P.A.,
Naaby-Hansen S.,
Stein R.,
Cramer R.,
Mollapour M.,
Workman P.,
Piper P.W.,
Pearl L.H.,
Prodromou C.;
"Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.";
Mol. Cell 10:1307-1318(2002).
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[19]
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SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K.,
Falvo J.V.,
Gerke L.C.,
Carroll A.S.,
Howson R.W.,
Weissman J.S.,
O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
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[20]
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LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S.,
Huh W.-K.,
Bower K.,
Howson R.W.,
Belle A.,
Dephoure N.,
O'Shea E.K.,
Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
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[21]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657 AND SER-663, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P.,
Smolka M.B.,
Payne S.H.,
Bafna V.,
Eng J.,
Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
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[22]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1038/nsb0697-477; PubMed=9187656 [NCBI, ExPASy, EBI, Israel, Japan]
Prodromou C.,
Roe S.M.,
Piper P.W.,
Pearl L.H.;
"A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone.";
Nat. Struct. Biol. 4:477-482(1997).
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[23]
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X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-214.
DOI=10.1016/S0092-8674(00)80314-1; PubMed=9230303 [NCBI, ExPASy, EBI, Israel, Japan]
Prodromou C.,
Roe S.M.,
O'Brien R.,
Ladbury J.E.,
Piper P.W.,
Pearl L.H.;
"Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.";
Cell 90:65-75(1997).
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[24]
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X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 273-560, AND MUTAGENESIS OF PHE-349; ARG-380 AND GLN-384.
DOI=10.1016/S1097-2765(03)00065-0; PubMed=12667448 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer P.,
Prodromou C.,
Hu B.,
Vaughan C.K.,
Roe S.M.,
Panaretou B.,
Piper P.W.,
Pearl L.H.;
"Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.";
Mol. Cell 11:647-658(2003).
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[25]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-214 IN COMPLEX WITH HUMAN CDC37.
DOI=10.1016/S0092-8674(03)01027-4; PubMed=14718169 [NCBI, ExPASy, EBI, Israel, Japan]
Roe S.M.,
Ali M.M.,
Meyer P.,
Vaughan C.K.,
Panaretou B.,
Piper P.W.,
Prodromou C.,
Pearl L.H.;
"The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37).";
Cell 116:87-98(2004).
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[26]
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X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 272-530 IN COMPLEX WITH AHA1, AND MUTAGENESIS OF LYS-387.
DOI=10.1038/sj.emboj.7600060; PubMed=14739935 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer P.;
"Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.";
EMBO J. 23:511-519(2004).
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[27]
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ERRATUM.
DOI=10.1038/sj.emboj.7600141; PubMed=15039704 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer P.,
Prodromou C.,
Liao C.,
Hu B.,
Mark Roe S.,
Vaughan C.K.,
Vlasic I.,
Panaretou B.,
Piper P.W.,
Pearl L.H.;
EMBO J. 23:1402-1410(2004).
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- FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.
- ENZYME REGULATION: Inhibited by geldanamycin, macbecin I and radicicol, which bind to the ATP-binding pocket. Co-chaperones CDC37, SBA1 and STI1 reduce ATPase activity. Co-chaperones AHA1 and HCH1 increase ATPase activity.
- SUBUNIT: Homodimer. Interacts with the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1 bind with their TPR repeats to the N-terminal pentapeptide MEEVD. Interacts directly with the substrates GCN2, HAP1 and STE11.
- INTERACTION:
O13585:-; NbExp=1; IntAct=EBI-8659, EBI-33008;
P25607:-; NbExp=1; IntAct=EBI-8659, EBI-22033;
P38272:-; NbExp=1; IntAct=EBI-8659, EBI-21600;
P47129:-; NbExp=1; IntAct=EBI-8659, EBI-25556;
Q12407:-; NbExp=1; IntAct=EBI-8659, EBI-33162;
Q06598:ACR3; NbExp=1; IntAct=EBI-8659, EBI-2122;
Q12449:AHA1; NbExp=2; IntAct=EBI-8659, EBI-37072;
P40074:AVT6; NbExp=1; IntAct=EBI-8659, EBI-22666;
P41815:BAP3; NbExp=1; IntAct=EBI-8659, EBI-3419;
P38356:BSD2; NbExp=1; IntAct=EBI-8659, EBI-3783;
Q16543:CDC37 (xeno); NbExp=1; IntAct=EBI-8659, EBI-295634;
P40558:CFD1; NbExp=1; IntAct=EBI-8659, EBI-24924;
P33313:CNS1; NbExp=1; IntAct=EBI-8659, EBI-4806;
P53951:COG5; NbExp=1; IntAct=EBI-8659, EBI-4841;
P53195:COG7; NbExp=1; IntAct=EBI-8659, EBI-4847;
Q04632:COG8; NbExp=1; IntAct=EBI-8659, EBI-6035;
P31381:FUN26; NbExp=1; IntAct=EBI-8659, EBI-7145;
P36125:GMH1; NbExp=1; IntAct=EBI-8659, EBI-26378;
P38720:GND1; NbExp=1; IntAct=EBI-8659, EBI-1965;
P40531:GVP36; NbExp=1; IntAct=EBI-8659, EBI-25006;
P46970:NMD5; NbExp=1; IntAct=EBI-8659, EBI-12084;
P21147:OLE1; NbExp=1; IntAct=EBI-8659, EBI-2098;
P46956:PHO86; NbExp=1; IntAct=EBI-8659, EBI-13337;
P51534:SHE4; NbExp=1; IntAct=EBI-8659, EBI-17086;
Q00772:SLT2; NbExp=1; IntAct=EBI-8659, EBI-17372;
Q07786:SOR2; NbExp=1; IntAct=EBI-8659, EBI-33572;
P40073:SSU81; NbExp=1; IntAct=EBI-8659, EBI-18140;
P25638:TAH1; NbExp=1; IntAct=EBI-8659, EBI-21956;
- SUBCELLULAR LOCATION: Cytoplasm.
- INDUCTION: Expressed constitutively and induced by high temperatures dependent on transcription factor HSF1. According to PubMed:2674684, it is constitutively expressed at low levels, however, due to the specificity of the antibody, this result is unsure.
- MISCELLANEOUS: Present with 444943 molecules/cell in log phase SD medium.
- SIMILARITY: Belongs to the heat shock protein 90 family.
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