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P31539

- HS104_YEAST

UniProt

P31539 - HS104_YEAST

Protein

Heat shock protein 104

Gene

HSP104

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].25 Publications

    Enzyme regulationi

    Inhibited by micromolar concentrations of guanidinium chloride. Inhibits the ATPase activity, but does not dissociate the hexameric protein.1 Publication

    Kineticsi

    1. KM=170 µM for ATP (at NBD1)5 Publications
    2. KM=4.7 µM for ATP (at NBD2)5 Publications

    Vmax=1.25 nmol/min/µg enzyme for ATP5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi212 – 2198ATP 1Sequence Analysis
    Nucleotide bindingi614 – 6218ATP 2Sequence Analysis

    GO - Molecular functioni

    1. ADP binding Source: SGD
    2. ATPase activity, coupled Source: SGD
    3. ATP binding Source: SGD
    4. chaperone binding Source: SGD
    5. unfolded protein binding Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular heat acclimation Source: SGD
    3. chaperone cofactor-dependent protein refolding Source: SGD
    4. inheritance of oxidatively modified proteins involved in replicative cell aging Source: SGD
    5. protein folding in endoplasmic reticulum Source: SGD
    6. protein unfolding Source: SGD
    7. trehalose metabolism in response to heat stress Source: SGD

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32130-MONOMER.
    SABIO-RKP31539.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein 104
    Alternative name(s):
    Protein aggregation-remodeling factor HSP104
    Gene namesi
    Name:HSP104
    Ordered Locus Names:YLL026W
    ORF Names:L0948
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLL026w.
    SGDiS000003949. HSP104.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Shuttles between the cytoplasm and the nucleus in an importin KAP95- and KAP121-dependent and an exportin XPO1-dependent manner. Accumulation in the nucleus is enhanced by severe heat shock. In the cytoplasm, concentrates on a perivacuolar compartment, the 'insoluble protein deposit' (IPOD), in which terminally aggregated proteins are sequestered. It is also found, to a lesser extend, at a 'juxtanuclear quality control' (JUNQ) compartment, where soluble ubiquitinated misfolded proteins accumulate.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD
    3. TRC complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi184 – 1841D → A, D, F, N, L, Q or S: Confers resistance to prion-curing by guanidine. 1 Publication
    Mutagenesisi184 – 1841D → K, W or Y: Impairs prion propagation. 1 Publication
    Mutagenesisi217 – 2171G → S: Largely reduces ATP hydrolysis. Alters bud morphology and causes septin mislocalization; when associated with I-499. 3 Publications
    Mutagenesisi217 – 2171G → V: Completely abolishes ATP hydrolysis. 3 Publications
    Mutagenesisi218 – 2181K → T: Abolishes substrate binding. Unable to confer thermotolerance. Reduces ATP hydrolysis by 98%; when associated with T-315. Comletely abolishes ATPase activity; when associated with T-620. 10 Publications
    Mutagenesisi257 – 2571Y → A: Reduces thermotolerance 10-fold. 1 Publication
    Mutagenesisi285 – 2851E → Q in HSP104(TRAP); completely abolishes ATP hydrolysis, but does not affect nucleotide binding, thus keeping HSP104 in an ATP-bound state; when associated with Q-687. 2 Publications
    Mutagenesisi315 – 3151A → T: Reduces ATP hydrolysis by 98%; when associated with T-218. 1 Publication
    Mutagenesisi317 – 3171T → A: Reduces rate of ATP hydrolysis at NBD1 nearly 10-fold. No effect on oligomerization. 2 Publications
    Mutagenesisi334 – 3341R → M: Reduces ATPase activity by 80%. Impairs oligomerization. 1 Publication
    Mutagenesisi419 – 4191R → M: Reduces ATPase activity by 80%. 1 Publication
    Mutagenesisi444 – 4441R → M: Reduces ATPase activity by 80%. 1 Publication
    Mutagenesisi462 – 4621L → R: Impairs prion propagation, but does not affect thermotolerance. 1 Publication
    Mutagenesisi495 – 4951R → M: Increases ATPase activity 3-fold. 1 Publication
    Mutagenesisi499 – 4991T → I: Reduces ATP hydrolysis by 50%. Alters bud morphology and causes septin mislocalization; when associated with S-217. 1 Publication
    Mutagenesisi503 – 5031A → V: Increases basal level of ATPase activity and abolishes stimulation of ATP hydrolysis upon substrate binding. Inhibits growth at 37 degrees Celsius. 2 Publications
    Mutagenesisi509 – 5091A → D: Reduces thermotolerance. 1 Publication
    Mutagenesisi557 – 5571P → L: Impairs prion propagation, but does not affect thermotolerance. 1 Publication
    Mutagenesisi619 – 6191G → V: Impairs oligomerization at low protein concentrations. 2 Publications
    Mutagenesisi620 – 6201K → T: Impairs oligomerization at low protein concentrations. Reduces ATP hydrolysis rate. Unable to confer thermotolerance. Comletely abolishes ATPase activity; when associated with T-218. 9 Publications
    Mutagenesisi621 – 6211T → A: Reduces ATP hydrolysis, but does not affect oligomerization. 1 Publication
    Mutagenesisi645 – 6451E → K: Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. 1 Publication
    Mutagenesisi662 – 6621Y → A or K: Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. 1 Publication
    Mutagenesisi662 – 6621Y → F or W: No effect. 1 Publication
    Mutagenesisi687 – 6871E → Q in HSP104(TRAP); completely abolishes ATP hydrolysis, but does not affect nucleotide binding, thus keeping HSP104 in an ATP-bound state; when associated with Q-285. 2 Publications
    Mutagenesisi704 – 7041D → N: Impairs prion propagation, but does not affect thermotolerance. 1 Publication
    Mutagenesisi728 – 7281N → A: Almost completely abolishes ATP hydrolysis at NBD2, but does not affect nucleotide binding, thus keeping NBD2 in an ATP-bound state. Reduces stimulation of ATP hydrolysis upon substrate binding. 4 Publications
    Mutagenesisi765 – 7651R → M: Can oligomerize in the absence of nucleotides. 1 Publication
    Mutagenesisi778 – 7781K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-782 and A-789. 1 Publication
    Mutagenesisi782 – 7821K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-778 and A-789. 1 Publication
    Mutagenesisi789 – 7891K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-778 and A-782. 1 Publication
    Mutagenesisi819 – 8191Y → W: Site-specific fluorescent probe in an otherwise Trp-less HSP104. Fluorescence of this Trp changes in response to ATP and ADP binding at NBD2. Has no effect on ATP hydrolysis or protein stability. 1 Publication
    Mutagenesisi826 – 8261R → M: Reduces ATP and ADP binding at NBD2 6-fold, but does not affect ATP hydrolysis at NBD2. Reduces catalytic rate at NBD1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 908908Heat shock protein 104PRO_0000191212Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei206 – 2061Phosphoserine2 Publications
    Modified residuei306 – 3061Phosphoserine1 Publication
    Modified residuei499 – 4991Phosphothreonine1 Publication
    Modified residuei535 – 5351Phosphoserine1 Publication
    Cross-linki620 – 620Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP31539.
    PaxDbiP31539.
    PeptideAtlasiP31539.

    2D gel databases

    SWISS-2DPAGEP31539.

    Expressioni

    Inductioni

    By heat stress dependent on the heat shock transcription factor HSF1 and the general stress transcription factors MSN2 and MSN4. Expressed at a higher level in respiring cells than in fermenting cells. Expressed in stationary phase cells and spores (at protein level).5 Publications

    Gene expression databases

    GenevestigatoriP31539.

    Interactioni

    Subunit structurei

    Homohexamer, forming a ring with a central pore. The hexamer is stabilized by high protein concentrations and by ADP or ATP. Oligomerization influences ATP hydrolysis activity at NBD2. Interacts with YDJ1. Interacts (via C-terminal DDLD tetrapeptide) with CNS1, CPR7 and STI1 (via TPR repeats); under respiratory growth conditions.8 Publications

    Protein-protein interaction databases

    BioGridi31226. 99 interactions.
    DIPiDIP-2252N.
    IntActiP31539. 14 interactions.
    MINTiMINT-530773.
    STRINGi4932.YLL026W.

    Structurei

    3D structure databases

    ProteinModelPortaliP31539.
    SMRiP31539. Positions 6-857.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni167 – 411245NBD1Add
    BLAST
    Regioni541 – 731191NBD2Add
    BLAST
    Regioni773 – 78917Nuclear localization signalAdd
    BLAST
    Regioni905 – 9084Interaction surface for TPR repeats

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili412 – 536125Sequence AnalysisAdd
    BLAST

    Domaini

    Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer, a low-affinity, high-turnover site (NBD1) and a high-affinity site (NBD2) with a 300-fold slower rate of hydrolysis. There is allosteric regulation between the 2 sites. ATP binding to NBD1 triggers binding of polypeptides and stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is crucial for oligomerization.
    The C-terminal extension is involved in oligomerization.

    Sequence similaritiesi

    Belongs to the ClpA/ClpB family.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG0542.
    GeneTreeiENSGT00390000012961.
    HOGENOMiHOG000218211.
    OMAiSNPCLIG.
    OrthoDBiEOG7X6M7K.

    Family and domain databases

    Gene3Di1.10.1780.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR019489. Clp_ATPase_C.
    IPR004176. Clp_N.
    IPR001270. ClpA/B.
    IPR018368. ClpA/B_CS1.
    IPR028299. ClpA/B_CS2.
    IPR023150. Dbl_Clp-N.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF07724. AAA_2. 1 hit.
    PF02861. Clp_N. 2 hits.
    PF10431. ClpB_D2-small. 1 hit.
    [Graphical view]
    PRINTSiPR00300. CLPPROTEASEA.
    SMARTiSM00382. AAA. 2 hits.
    SM01086. ClpB_D2-small. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00870. CLPAB_1. 1 hit.
    PS00871. CLPAB_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P31539-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDQTQFTER ALTILTLAQK LASDHQHPQL QPIHILAAFI ETPEDGSVPY    50
    LQNLIEKGRY DYDLFKKVVN RNLVRIPQQQ PAPAEITPSY ALGKVLQDAA 100
    KIQKQQKDSF IAQDHILFAL FNDSSIQQIF KEAQVDIEAI KQQALELRGN 150
    TRIDSRGADT NTPLEYLSKY AIDMTEQARQ GKLDPVIGRE EEIRSTIRVL 200
    ARRIKSNPCL IGEPGIGKTA IIEGVAQRII DDDVPTILQG AKLFSLDLAA 250
    LTAGAKYKGD FEERFKGVLK EIEESKTLIV LFIDEIHMLM GNGKDDAANI 300
    LKPALSRGQL KVIGATTNNE YRSIVEKDGA FERRFQKIEV AEPSVRQTVA 350
    ILRGLQPKYE IHHGVRILDS ALVTAAQLAK RYLPYRRLPD SALDLVDISC 400
    AGVAVARDSK PEELDSKERQ LQLIQVEIKA LERDEDADST TKDRLKLARQ 450
    KEASLQEELE PLRQRYNEEK HGHEELTQAK KKLDELENKA LDAERRYDTA 500
    TAADLRYFAI PDIKKQIEKL EDQVAEEERR AGANSMIQNV VDSDTISETA 550
    ARLTGIPVKK LSESENEKLI HMERDLSSEV VGQMDAIKAV SNAVRLSRSG 600
    LANPRQPASF LFLGLSGSGK TELAKKVAGF LFNDEDMMIR VDCSELSEKY 650
    AVSKLLGTTA GYVGYDEGGF LTNQLQYKPY SVLLFDEVEK AHPDVLTVML 700
    QMLDDGRITS GQGKTIDCSN CIVIMTSNLG AEFINSQQGS KIQESTKNLV 750
    MGAVRQHFRP EFLNRISSIV IFNKLSRKAI HKIVDIRLKE IEERFEQNDK 800
    HYKLNLTQEA KDFLAKYGYS DDMGARPLNR LIQNEILNKL ALRILKNEIK 850
    DKETVNVVLK KGKSRDENVP EEAEECLEVL PNHEATIGAD TLGDDDNEDS 900
    MEIDDDLD 908
    Length:908
    Mass (Da):102,035
    Last modified:February 1, 1996 - v2
    Checksum:i4AD0E7E3AF98E318
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M67479 Genomic DNA. Translation: AAA50477.1.
    Z73131 Genomic DNA. Translation: CAA97475.1.
    Z73130 Genomic DNA. Translation: CAA97474.1.
    AY693002 Genomic DNA. Translation: AAT93021.1.
    X97560 Genomic DNA. Translation: CAA66164.1.
    BK006945 Genomic DNA. Translation: DAA09294.1.
    PIRiS61476.
    RefSeqiNP_013074.1. NM_001181846.1.

    Genome annotation databases

    EnsemblFungiiYLL026W; YLL026W; YLL026W.
    GeneIDi850633.
    KEGGisce:YLL026W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M67479 Genomic DNA. Translation: AAA50477.1 .
    Z73131 Genomic DNA. Translation: CAA97475.1 .
    Z73130 Genomic DNA. Translation: CAA97474.1 .
    AY693002 Genomic DNA. Translation: AAT93021.1 .
    X97560 Genomic DNA. Translation: CAA66164.1 .
    BK006945 Genomic DNA. Translation: DAA09294.1 .
    PIRi S61476.
    RefSeqi NP_013074.1. NM_001181846.1.

    3D structure databases

    ProteinModelPortali P31539.
    SMRi P31539. Positions 6-857.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31226. 99 interactions.
    DIPi DIP-2252N.
    IntActi P31539. 14 interactions.
    MINTi MINT-530773.
    STRINGi 4932.YLL026W.

    2D gel databases

    SWISS-2DPAGE P31539.

    Proteomic databases

    MaxQBi P31539.
    PaxDbi P31539.
    PeptideAtlasi P31539.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLL026W ; YLL026W ; YLL026W .
    GeneIDi 850633.
    KEGGi sce:YLL026W.

    Organism-specific databases

    CYGDi YLL026w.
    SGDi S000003949. HSP104.

    Phylogenomic databases

    eggNOGi COG0542.
    GeneTreei ENSGT00390000012961.
    HOGENOMi HOG000218211.
    OMAi SNPCLIG.
    OrthoDBi EOG7X6M7K.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32130-MONOMER.
    SABIO-RK P31539.

    Miscellaneous databases

    NextBioi 966553.
    PROi P31539.

    Gene expression databases

    Genevestigatori P31539.

    Family and domain databases

    Gene3Di 1.10.1780.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR019489. Clp_ATPase_C.
    IPR004176. Clp_N.
    IPR001270. ClpA/B.
    IPR018368. ClpA/B_CS1.
    IPR028299. ClpA/B_CS2.
    IPR023150. Dbl_Clp-N.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF07724. AAA_2. 1 hit.
    PF02861. Clp_N. 2 hits.
    PF10431. ClpB_D2-small. 1 hit.
    [Graphical view ]
    PRINTSi PR00300. CLPPROTEASEA.
    SMARTi SM00382. AAA. 2 hits.
    SM01086. ClpB_D2-small. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00870. CLPAB_1. 1 hit.
    PS00871. CLPAB_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Hsp104 is a highly conserved protein with two essential nucleotide-binding sites."
      Parsell D.A., Sanchez Y., Stitzel J.D., Lindquist S.L.
      Nature 353:270-273(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-218 AND LYS-620.
      Strain: ATCC 26109 / X2180 / NCYC 826.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "The sequence of 32kb on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABC transporter homologous to the human multidrug resistance protein."
      Purnelle B., Goffeau A.
      Yeast 13:183-188(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 749-908.
      Strain: ATCC 204508 / S288c.
    6. "HSP104 required for induced thermotolerance."
      Sanchez Y., Lindquist S.L.
      Science 248:1112-1115(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Hsp104 is required for tolerance to many forms of stress."
      Sanchez Y., Taulien J., Borkovich K.A., Lindquist S.L.
      EMBO J. 11:2357-2364(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    8. "Genetic evidence for a functional relationship between Hsp104 and Hsp70."
      Sanchez Y., Parsell D.A., Taulien J., Vogel J.L., Craig E.A., Lindquist S.L.
      J. Bacteriol. 175:6484-6491(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes."
      Parsell D.A., Kowal A.S., Lindquist S.L.
      J. Biol. Chem. 269:4480-4487(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, MUTAGENESIS OF LYS-218 AND LYS-620, SUBUNIT, ELECTRON MICROSCOPY.
    10. "Protein disaggregation mediated by heat-shock protein Hsp104."
      Parsell D.A., Kowal A.S., Singer M.A., Lindquist S.L.
      Nature 372:475-478(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]."
      Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G., Liebman S.W.
      Science 268:880-884(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION MAINTENANCE.
    12. "Heat-shock protein 104 expression is sufficient for thermotolerance in yeast."
      Lindquist S.L., Kim G.
      Proc. Natl. Acad. Sci. U.S.A. 93:5301-5306(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    13. "Hsp104 responds to heat and oxidative stress with different intracellular localization in Saccharomyces cerevisiae."
      Fujita K., Kawai R., Iwahashi H., Komatsu Y.
      Biochem. Biophys. Res. Commun. 248:542-547(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins."
      Glover J.R., Lindquist S.L.
      Cell 94:73-82(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YDJ1.
    15. "The ATPase activity of Hsp104, effects of environmental conditions and mutations."
      Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S.L.
      J. Biol. Chem. 273:15546-15552(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-217; LYS-218; GLY-619 AND LYS-620.
    16. Erratum
      Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S.L.
      J. Biol. Chem. 273:19922-19922(1998)
    17. "Purification and properties of Hsp104 from yeast."
      Schirmer E.C., Lindquist S.L.
      Methods Enzymol. 290:430-444(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    18. "Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopy."
      Kawai R., Fujita K., Iwahashi H., Komatsu Y.
      Cell Stress Chaperones 4:46-53(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    19. "Rnq1: an epigenetic modifier of protein function in yeast."
      Sondheimer N., Lindquist S.L.
      Mol. Cell 5:163-172(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION PROPAGATION.
    20. "[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p."
      Moriyama H., Edskes H.K., Wickner R.B.
      Mol. Cell. Biol. 20:8916-8922(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION PROPAGATION.
    21. "Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions."
      Jung G., Masison D.C.
      Curr. Microbiol. 43:7-10(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION PROPAGATION.
    22. "Hsp104 interacts with Hsp90 cochaperones in respiring yeast."
      Abbas-Terki T., Donze O., Briand P.-A., Picard D.
      Mol. Cell. Biol. 21:7569-7575(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNS1; CPR7 AND STI1.
    23. "The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation."
      Ferreira P.C., Ness F., Edwards S.R., Cox B.S., Tuite M.F.
      Mol. Microbiol. 40:1357-1369(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION PROPAGATION, MUTAGENESIS OF LYS-218 AND LYS-620.
    24. "Subunit interactions influence the biochemical and biological properties of Hsp104."
      Schirmer E.C., Ware D.M., Queitsch C., Kowal A.S., Lindquist S.L.
      Proc. Natl. Acad. Sci. U.S.A. 98:914-919(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLY-217; LYS-218; GLY-619; LYS-620 AND THR-621.
    25. "Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants."
      Hattendorf D.A., Lindquist S.L.
      EMBO J. 21:12-21(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF THR-317 AND ASN-728.
    26. "Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein."
      Cashikar A.G., Schirmer E.C., Hattendorf D.A., Glover J.R., Ramakrishnan M.S., Ware D.M., Lindquist S.L.
      Mol. Cell 9:751-760(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE-BINDING, MUTAGENESIS OF LYS-218; ALA-315; ALA-503 AND ASN-728.
    27. "Guanidine hydrochloride inhibits the generation of prion 'seeds' but not prion protein aggregation in yeast."
      Ness F., Ferreira P.C., Cox B.S., Tuite M.F.
      Mol. Cell. Biol. 22:5593-5605(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION PROPAGATION, MUTAGENESIS OF LYS-218 AND LYS-620.
    28. "HSF and Msn2/4p can exclusively or cooperatively activate the yeast HSP104 gene."
      Grably M.R., Stanhill A., Tell O., Engelberg D.
      Mol. Microbiol. 44:21-35(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    29. "Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding."
      Hattendorf D.A., Lindquist S.L.
      Proc. Natl. Acad. Sci. U.S.A. 99:2732-2737(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-819 AND ARG-826, ATP-BINDING.
    30. "Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance."
      Jung G., Jones G., Masison D.C.
      Proc. Natl. Acad. Sci. U.S.A. 99:9936-9941(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-184.
    31. "Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104."
      Kryndushkin D.S., Alexandrov I.M., Ter-Avanesyan M.D., Kushnirov V.V.
      J. Biol. Chem. 278:49636-49643(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION FRAGMENTATION.
    32. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    33. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    34. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
      Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-620.
    35. "The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104."
      Grimminger V., Richter K., Imhof A., Buchner J., Walter S.
      J. Biol. Chem. 279:7378-7383(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    36. "Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104."
      Lum R., Tkach J.M., Vierling E., Glover J.R.
      J. Biol. Chem. 279:29139-29146(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-257; GLU-645 AND TYR-662, BIOPHYSICOCHEMICAL PROPERTIES.
    37. "Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region."
      Schirmer E.C., Homann O.R., Kowal A.S., Lindquist S.L.
      Mol. Biol. Cell 15:2061-2072(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-217; THR-499; ALA-503 AND ALA-509.
    38. "Upregulation of the Hsp104 chaperone at physiological temperature during recovery from thermal insult."
      Seppae L., Haenninen A.-L., Makarow M.
      Mol. Microbiol. 52:217-225(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    39. "Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers."
      Shorter J., Lindquist S.L.
      Science 304:1793-1797(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION PROPAGATION.
    40. "Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104."
      Haslbeck M., Miess A., Stromer T., Walter S., Buchner J.
      J. Biol. Chem. 280:23861-23868(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    41. "A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104."
      Cashikar A.G., Duennwald M., Lindquist S.L.
      J. Biol. Chem. 280:23869-23875(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    42. Erratum
      Cashikar A.G., Duennwald M., Lindquist S.L.
      J. Biol. Chem. 281:8996-8996(2006)
    43. "Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides."
      Boesl B., Grimminger V., Walter S.
      J. Biol. Chem. 280:38170-38176(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, MUTAGENESIS OF LYS-218; GLU-285; LYS-620 AND GLU-687.
    44. "Yeast prion-protein, sup35, fibril formation proceeds by addition and substraction of oligomers."
      Narayanan S., Walter S., Reif B.
      ChemBioChem 7:757-765(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION DISASSEMBLY.
    45. "Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities."
      Shorter J., Lindquist S.L.
      Mol. Cell 23:425-438(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION DISASSEMBLY.
    46. "Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104."
      Wendler P., Shorter J., Plisson C., Cashikar A.G., Lindquist S.L., Saibil H.R.
      Cell 131:1366-1377(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, ELECTRON MICROSCOPY, MUTAGENESIS OF ARG-334; ARG-419; ARG-444; ARG-495; ASN-728 AND ARG-765.
    47. "Processing of proteins by the molecular chaperone Hsp104."
      Schaupp A., Marcinowski M., Grimminger V., Boesl B., Walter S.
      J. Mol. Biol. 370:674-686(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-218; GLU-285; LYS-620 AND GLU-687.
    48. "Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation."
      Kurahashi H., Nakamura Y.
      Mol. Microbiol. 63:1669-1683(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION PROPAGATION, MUTAGENESIS OF LEU-462; PRO-557 AND ASP-704.
    49. "Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity."
      Doyle S.M., Shorter J., Zolkiewski M., Hoskins J.R., Lindquist S.L., Wickner S.
      Nat. Struct. Mol. Biol. 14:114-122(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-218; THR-317; LYS-620 AND ASN-728.
    50. "Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance."
      Satpute-Krishnan P., Langseth S.X., Serio T.R.
      PLoS Biol. 5:251-262(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRION PROPAGATION.
    51. "The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly."
      Mackay R.G., Helsen C.W., Tkach J.M., Glover J.R.
      Biochemistry 47:1918-1927(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CPR7.
    52. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-306; THR-499 AND SER-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    53. "Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation."
      Tessarz P., Mogk A., Bukau B.
      Mol. Microbiol. 68:87-97(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    54. "Misfolded proteins partition between two distinct quality control compartments."
      Kaganovich D., Kopito R., Frydman J.
      Nature 454:1088-1095(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    55. "Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells."
      Tkach J.M., Glover J.R.
      Traffic 9:39-56(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-778; LYS-782 AND LYS-789.
    56. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    57. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    58. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHS104_YEAST
    AccessioniPrimary (citable) accession number: P31539
    Secondary accession number(s): D6VXX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 32800 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3