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P31539 (HS104_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock protein 104
Alternative name(s):
Protein aggregation-remodeling factor HSP104
Gene names
Name:HSP104
Ordered Locus Names:YLL026W
ORF Names:L0948
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length908 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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+]. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.27 Ref.31 Ref.36 Ref.39 Ref.40 Ref.41 Ref.44 Ref.45 Ref.47 Ref.48 Ref.49 Ref.50 Ref.53

Enzyme regulation

Inhibited by micromolar concentrations of guanidinium chloride. Inhibits the ATPase activity, but does not dissociate the hexameric protein. Ref.35

Subunit structure

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. Ref.9 Ref.14 Ref.17 Ref.22 Ref.24 Ref.43 Ref.46 Ref.51

Subcellular location

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. Ref.13 Ref.18 Ref.32 Ref.54 Ref.55

Induction

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). Ref.7 Ref.9 Ref.12 Ref.28 Ref.35 Ref.38

Domain

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.

Miscellaneous

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

Sequence similarities

Belongs to the ClpA/ClpB family.

Biophysicochemical properties

Kinetic parameters:

KM=170 µM for ATP (at NBD1) Ref.15 Ref.17 Ref.24 Ref.25 Ref.36

KM=4.7 µM for ATP (at NBD2)

Vmax=1.25 nmol/min/µg enzyme for ATP

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Nucleus
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.43. Source: GOC

cellular heat acclimation

Inferred from mutant phenotype Ref.6. Source: SGD

chaperone cofactor-dependent protein refolding

Inferred from direct assay Ref.14. Source: SGD

inheritance of oxidatively modified proteins involved in replicative cell aging

Inferred from mutant phenotype PubMed 17908928. Source: SGD

protein folding in endoplasmic reticulum

Inferred from mutant phenotype PubMed 10931304. Source: SGD

protein unfolding

Inferred from mutant phenotype Ref.10. Source: SGD

trehalose metabolism in response to heat stress

Inferred from mutant phenotype PubMed 9797333. Source: SGD

   Cellular_componentTRC complex

Inferred from direct assay PubMed 20850366. Source: SGD

cytoplasm

Inferred from direct assay Ref.18. Source: SGD

nucleus

Inferred from direct assay Ref.18. Source: SGD

   Molecular_functionADP binding

Inferred from mutant phenotype Ref.29. Source: SGD

ATP binding

Inferred from mutant phenotype Ref.29. Source: SGD

ATPase activity, coupled

Inferred from direct assay Ref.43. Source: SGD

chaperone binding

Inferred from direct assay Ref.14. Source: SGD

unfolded protein binding

Inferred from direct assay Ref.43. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 908908Heat shock protein 104
PRO_0000191212

Regions

Nucleotide binding212 – 2198ATP 1 Potential
Nucleotide binding614 – 6218ATP 2 Potential
Region167 – 411245NBD1
Region541 – 731191NBD2
Region773 – 78917Nuclear localization signal
Region905 – 9084Interaction surface for TPR repeats
Coiled coil412 – 536125 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.57
Modified residue2061Phosphoserine Ref.52 Ref.56
Modified residue3061Phosphoserine Ref.52
Modified residue4991Phosphothreonine Ref.52
Modified residue5351Phosphoserine Ref.52
Cross-link620Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.34

Experimental info

Mutagenesis1841D → A, D, F, N, L, Q or S: Confers resistance to prion-curing by guanidine. Ref.30
Mutagenesis1841D → K, W or Y: Impairs prion propagation. Ref.30
Mutagenesis2171G → S: Largely reduces ATP hydrolysis. Alters bud morphology and causes septin mislocalization; when associated with I-499. Ref.15 Ref.24 Ref.37
Mutagenesis2171G → V: Completely abolishes ATP hydrolysis. Ref.15 Ref.24 Ref.37
Mutagenesis2181K → 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. Ref.1 Ref.9 Ref.15 Ref.23 Ref.24 Ref.26 Ref.27 Ref.43 Ref.47 Ref.49
Mutagenesis2571Y → A: Reduces thermotolerance 10-fold. Ref.36
Mutagenesis2851E → 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. Ref.43 Ref.47
Mutagenesis3151A → T: Reduces ATP hydrolysis by 98%; when associated with T-218. Ref.26
Mutagenesis3171T → A: Reduces rate of ATP hydrolysis at NBD1 nearly 10-fold. No effect on oligomerization. Ref.25 Ref.49
Mutagenesis3341R → M: Reduces ATPase activity by 80%. Impairs oligomerization. Ref.46
Mutagenesis4191R → M: Reduces ATPase activity by 80%. Ref.46
Mutagenesis4441R → M: Reduces ATPase activity by 80%. Ref.46
Mutagenesis4621L → R: Impairs prion propagation, but does not affect thermotolerance. Ref.48
Mutagenesis4951R → M: Increases ATPase activity 3-fold. Ref.46
Mutagenesis4991T → I: Reduces ATP hydrolysis by 50%. Alters bud morphology and causes septin mislocalization; when associated with S-217. Ref.37
Mutagenesis5031A → V: Increases basal level of ATPase activity and abolishes stimulation of ATP hydrolysis upon substrate binding. Inhibits growth at 37 degrees Celsius. Ref.26 Ref.37
Mutagenesis5091A → D: Reduces thermotolerance. Ref.37
Mutagenesis5571P → L: Impairs prion propagation, but does not affect thermotolerance. Ref.48
Mutagenesis6191G → V: Impairs oligomerization at low protein concentrations. Ref.15 Ref.24
Mutagenesis6201K → T: Impairs oligomerization at low protein concentrations. Reduces ATP hydrolysis rate. Unable to confer thermotolerance. Comletely abolishes ATPase activity; when associated with T-218. Ref.1 Ref.9 Ref.15 Ref.23 Ref.24 Ref.27 Ref.43 Ref.47 Ref.49
Mutagenesis6211T → A: Reduces ATP hydrolysis, but does not affect oligomerization. Ref.24
Mutagenesis6451E → K: Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. Ref.36
Mutagenesis6621Y → A or K: Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. Ref.36
Mutagenesis6621Y → F or W: No effect. Ref.36
Mutagenesis6871E → 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. Ref.43 Ref.47
Mutagenesis7041D → N: Impairs prion propagation, but does not affect thermotolerance. Ref.48
Mutagenesis7281N → 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. Ref.25 Ref.26 Ref.46 Ref.49
Mutagenesis7651R → M: Can oligomerize in the absence of nucleotides. Ref.46
Mutagenesis7781K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-782 and A-789. Ref.55
Mutagenesis7821K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-778 and A-789. Ref.55
Mutagenesis7891K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-778 and A-782. Ref.55
Mutagenesis8191Y → 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. Ref.29
Mutagenesis8261R → M: Reduces ATP and ADP binding at NBD2 6-fold, but does not affect ATP hydrolysis at NBD2. Reduces catalytic rate at NBD1. Ref.29

Sequences

Sequence LengthMass (Da)Tools
P31539 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 4AD0E7E3AF98E318

FASTA908102,035
        10         20         30         40         50         60 
MNDQTQFTER ALTILTLAQK LASDHQHPQL QPIHILAAFI ETPEDGSVPY LQNLIEKGRY 

        70         80         90        100        110        120 
DYDLFKKVVN RNLVRIPQQQ PAPAEITPSY ALGKVLQDAA KIQKQQKDSF IAQDHILFAL 

       130        140        150        160        170        180 
FNDSSIQQIF KEAQVDIEAI KQQALELRGN TRIDSRGADT NTPLEYLSKY AIDMTEQARQ 

       190        200        210        220        230        240 
GKLDPVIGRE EEIRSTIRVL ARRIKSNPCL IGEPGIGKTA IIEGVAQRII DDDVPTILQG 

       250        260        270        280        290        300 
AKLFSLDLAA LTAGAKYKGD FEERFKGVLK EIEESKTLIV LFIDEIHMLM GNGKDDAANI 

       310        320        330        340        350        360 
LKPALSRGQL KVIGATTNNE YRSIVEKDGA FERRFQKIEV AEPSVRQTVA ILRGLQPKYE 

       370        380        390        400        410        420 
IHHGVRILDS ALVTAAQLAK RYLPYRRLPD SALDLVDISC AGVAVARDSK PEELDSKERQ 

       430        440        450        460        470        480 
LQLIQVEIKA LERDEDADST TKDRLKLARQ KEASLQEELE PLRQRYNEEK HGHEELTQAK 

       490        500        510        520        530        540 
KKLDELENKA LDAERRYDTA TAADLRYFAI PDIKKQIEKL EDQVAEEERR AGANSMIQNV 

       550        560        570        580        590        600 
VDSDTISETA ARLTGIPVKK LSESENEKLI HMERDLSSEV VGQMDAIKAV SNAVRLSRSG 

       610        620        630        640        650        660 
LANPRQPASF LFLGLSGSGK TELAKKVAGF LFNDEDMMIR VDCSELSEKY AVSKLLGTTA 

       670        680        690        700        710        720 
GYVGYDEGGF LTNQLQYKPY SVLLFDEVEK AHPDVLTVML QMLDDGRITS GQGKTIDCSN 

       730        740        750        760        770        780 
CIVIMTSNLG AEFINSQQGS KIQESTKNLV MGAVRQHFRP EFLNRISSIV IFNKLSRKAI 

       790        800        810        820        830        840 
HKIVDIRLKE IEERFEQNDK HYKLNLTQEA KDFLAKYGYS DDMGARPLNR LIQNEILNKL 

       850        860        870        880        890        900 
ALRILKNEIK DKETVNVVLK KGKSRDENVP EEAEECLEVL PNHEATIGAD TLGDDDNEDS 


MEIDDDLD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[33]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS61476.
RefSeqNP_013074.1. NM_001181846.1.

3D structure databases

ProteinModelPortalP31539.
SMRP31539. Positions 6-857.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31226. 99 interactions.
DIPDIP-2252N.
IntActP31539. 14 interactions.
MINTMINT-530773.
STRING4932.YLL026W.

2D gel databases

SWISS-2DPAGEP31539.

Proteomic databases

MaxQBP31539.
PaxDbP31539.
PeptideAtlasP31539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLL026W; YLL026W; YLL026W.
GeneID850633.
KEGGsce:YLL026W.

Organism-specific databases

CYGDYLL026w.
SGDS000003949. HSP104.

Phylogenomic databases

eggNOGCOG0542.
GeneTreeENSGT00390000012961.
HOGENOMHOG000218211.
OMASNPCLIG.
OrthoDBEOG7X6M7K.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP31539.

Family and domain databases

Gene3D1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR003593. 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]
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966553.
PROP31539.

Entry information

Entry nameHS104_YEAST
AccessionPrimary (citable) accession number: P31539
Secondary accession number(s): D6VXX8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families