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Heat shock protein 104 (Protein aggregation-remodeling factor HSP104)

 HS104_YEAST             Reviewed;         908 AA.
P31539; D6VXX8;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
25-OCT-2017, entry version 165.
RecName: Full=Heat shock protein 104;
AltName: Full=Protein aggregation-remodeling factor HSP104;
Name=HSP104; OrderedLocusNames=YLL026W; ORFNames=L0948;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LYS-218 AND
LYS-620.
STRAIN=ATCC 26109 / X2180 / NCYC 826;
PubMed=1896074; DOI=10.1038/353270a0;
Parsell D.A., Sanchez Y., Stitzel J.D., Lindquist S.L.;
"Hsp104 is a highly conserved protein with two essential nucleotide-
binding sites.";
Nature 353:270-273(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
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., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 749-908.
STRAIN=ATCC 204508 / S288c;
PubMed=9046100;
DOI=10.1002/(SICI)1097-0061(199702)13:2<183::AID-YEA65>3.0.CO;2-V;
Purnelle B., Goffeau A.;
"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.";
Yeast 13:183-188(1997).
[6]
FUNCTION.
PubMed=2188365; DOI=10.1126/science.2188365;
Sanchez Y., Lindquist S.L.;
"HSP104 required for induced thermotolerance.";
Science 248:1112-1115(1990).
[7]
FUNCTION, AND INDUCTION.
PubMed=1600951;
Sanchez Y., Taulien J., Borkovich K.A., Lindquist S.L.;
"Hsp104 is required for tolerance to many forms of stress.";
EMBO J. 11:2357-2364(1992).
[8]
FUNCTION.
PubMed=8407824; DOI=10.1128/jb.175.20.6484-6491.1993;
Sanchez Y., Parsell D.A., Taulien J., Vogel J.L., Craig E.A.,
Lindquist S.L.;
"Genetic evidence for a functional relationship between Hsp104 and
Hsp70.";
J. Bacteriol. 175:6484-6491(1993).
[9]
INDUCTION, MUTAGENESIS OF LYS-218 AND LYS-620, SUBUNIT, AND ELECTRON
MICROSCOPY.
PubMed=8308017;
Parsell D.A., Kowal A.S., Lindquist S.L.;
"Saccharomyces cerevisiae Hsp104 protein. Purification and
characterization of ATP-induced structural changes.";
J. Biol. Chem. 269:4480-4487(1994).
[10]
FUNCTION.
PubMed=7984243; DOI=10.1038/372475a0;
Parsell D.A., Kowal A.S., Singer M.A., Lindquist S.L.;
"Protein disaggregation mediated by heat-shock protein Hsp104.";
Nature 372:475-478(1994).
[11]
FUNCTION IN PRION MAINTENANCE.
PubMed=7754373; DOI=10.1126/science.7754373;
Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G.,
Liebman S.W.;
"Role of the chaperone protein Hsp104 in propagation of the yeast
prion-like factor [psi+].";
Science 268:880-884(1995).
[12]
FUNCTION, AND INDUCTION.
PubMed=8643570; DOI=10.1073/pnas.93.11.5301;
Lindquist S.L., Kim G.;
"Heat-shock protein 104 expression is sufficient for thermotolerance
in yeast.";
Proc. Natl. Acad. Sci. U.S.A. 93:5301-5306(1996).
[13]
SUBCELLULAR LOCATION.
PubMed=9703962; DOI=10.1006/bbrc.1998.9008;
Fujita K., Kawai R., Iwahashi H., Komatsu Y.;
"Hsp104 responds to heat and oxidative stress with different
intracellular localization in Saccharomyces cerevisiae.";
Biochem. Biophys. Res. Commun. 248:542-547(1998).
[14]
FUNCTION, AND INTERACTION WITH YDJ1.
PubMed=9674429; DOI=10.1016/S0092-8674(00)81223-4;
Glover J.R., Lindquist S.L.;
"Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues
previously aggregated proteins.";
Cell 94:73-82(1998).
[15]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-217; LYS-218;
GLY-619 AND LYS-620.
PubMed=9624144; DOI=10.1074/jbc.273.25.15546;
Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S.L.;
"The ATPase activity of Hsp104, effects of environmental conditions
and mutations.";
J. Biol. Chem. 273:15546-15552(1998).
[16]
ERRATUM.
Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S.L.;
J. Biol. Chem. 273:19922-19922(1998).
[17]
FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9534180; DOI=10.1016/S0076-6879(98)90036-2;
Schirmer E.C., Lindquist S.L.;
"Purification and properties of Hsp104 from yeast.";
Methods Enzymol. 290:430-444(1998).
[18]
SUBCELLULAR LOCATION.
PubMed=10467108; DOI=10.1054/csac.1999.0076;
Kawai R., Fujita K., Iwahashi H., Komatsu Y.;
"Direct evidence for the intracellular localization of Hsp104 in
Saccharomyces cerevisiae by immunoelectron microscopy.";
Cell Stress Chaperones 4:46-53(1999).
[19]
FUNCTION IN PRION PROPAGATION.
PubMed=10678178; DOI=10.1016/S1097-2765(00)80412-8;
Sondheimer N., Lindquist S.L.;
"Rnq1: an epigenetic modifier of protein function in yeast.";
Mol. Cell 5:163-172(2000).
[20]
FUNCTION IN PRION PROPAGATION.
PubMed=11073991; DOI=10.1128/MCB.20.23.8916-8922.2000;
Moriyama H., Edskes H.K., Wickner R.B.;
"[URE3] prion propagation in Saccharomyces cerevisiae: requirement for
chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.";
Mol. Cell. Biol. 20:8916-8922(2000).
[21]
FUNCTION IN PRION PROPAGATION.
PubMed=11375656; DOI=10.1007/s002840010251;
Jung G., Masison D.C.;
"Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible
explanation for its effect in curing yeast prions.";
Curr. Microbiol. 43:7-10(2001).
[22]
INTERACTION WITH CNS1; CPR7 AND STI1.
PubMed=11604493; DOI=10.1128/MCB.21.22.7569-7575.2001;
Abbas-Terki T., Donze O., Briand P.-A., Picard D.;
"Hsp104 interacts with Hsp90 cochaperones in respiring yeast.";
Mol. Cell. Biol. 21:7569-7575(2001).
[23]
FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LYS-218 AND LYS-620.
PubMed=11442834; DOI=10.1046/j.1365-2958.2001.02478.x;
Ferreira P.C., Ness F., Edwards S.R., Cox B.S., Tuite M.F.;
"The elimination of the yeast [PSI+] prion by guanidine hydrochloride
is the result of Hsp104 inactivation.";
Mol. Microbiol. 40:1357-1369(2001).
[24]
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF GLY-217;
LYS-218; GLY-619; LYS-620 AND THR-621.
PubMed=11158570; DOI=10.1073/pnas.98.3.914;
Schirmer E.C., Ware D.M., Queitsch C., Kowal A.S., Lindquist S.L.;
"Subunit interactions influence the biochemical and biological
properties of Hsp104.";
Proc. Natl. Acad. Sci. U.S.A. 98:914-919(2001).
[25]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF THR-317 AND ASN-728.
PubMed=11782421; DOI=10.1093/emboj/21.1.12;
Hattendorf D.A., Lindquist S.L.;
"Cooperative kinetics of both Hsp104 ATPase domains and interdomain
communication revealed by AAA sensor-1 mutants.";
EMBO J. 21:12-21(2002).
[26]
SUBSTRATE-BINDING, AND MUTAGENESIS OF LYS-218; ALA-315; ALA-503 AND
ASN-728.
PubMed=11983167; DOI=10.1016/S1097-2765(02)00499-9;
Cashikar A.G., Schirmer E.C., Hattendorf D.A., Glover J.R.,
Ramakrishnan M.S., Ware D.M., Lindquist S.L.;
"Defining a pathway of communication from the C-terminal peptide
binding domain to the N-terminal ATPase domain in a AAA protein.";
Mol. Cell 9:751-760(2002).
[27]
FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LYS-218 AND LYS-620.
PubMed=12101251; DOI=10.1128/MCB.22.15.5593-5605.2002;
Ness F., Ferreira P.C., Cox B.S., Tuite M.F.;
"Guanidine hydrochloride inhibits the generation of prion 'seeds' but
not prion protein aggregation in yeast.";
Mol. Cell. Biol. 22:5593-5605(2002).
[28]
INDUCTION.
PubMed=11967066; DOI=10.1046/j.1365-2958.2002.02860.x;
Grably M.R., Stanhill A., Tell O., Engelberg D.;
"HSF and Msn2/4p can exclusively or cooperatively activate the yeast
HSP104 gene.";
Mol. Microbiol. 44:21-35(2002).
[29]
MUTAGENESIS OF TYR-819 AND ARG-826, AND ATP-BINDING.
PubMed=11867765; DOI=10.1073/pnas.261693199;
Hattendorf D.A., Lindquist S.L.;
"Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of
Hsp104 with a site-specific fluorescent probe of nucleotide binding.";
Proc. Natl. Acad. Sci. U.S.A. 99:2732-2737(2002).
[30]
MUTAGENESIS OF ASP-184.
PubMed=12105276; DOI=10.1073/pnas.152333299;
Jung G., Jones G., Masison D.C.;
"Amino acid residue 184 of yeast Hsp104 chaperone is critical for
prion-curing by guanidine, prion propagation, and thermotolerance.";
Proc. Natl. Acad. Sci. U.S.A. 99:9936-9941(2002).
[31]
FUNCTION IN PRION FRAGMENTATION.
PubMed=14507919; DOI=10.1074/jbc.M307996200;
Kryndushkin D.S., Alexandrov I.M., Ter-Avanesyan M.D., Kushnirov V.V.;
"Yeast [PSI+] prion aggregates are formed by small Sup35 polymers
fragmented by Hsp104.";
J. Biol. Chem. 278:49636-49643(2003).
[32]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
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).
[33]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
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).
[34]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-620, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=14557538; DOI=10.1073/pnas.2135500100;
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response
to mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[35]
ENZYME REGULATION.
PubMed=14668331; DOI=10.1074/jbc.M312403200;
Grimminger V., Richter K., Imhof A., Buchner J., Walter S.;
"The prion curing agent guanidinium chloride specifically inhibits ATP
hydrolysis by Hsp104.";
J. Biol. Chem. 279:7378-7383(2004).
[36]
FUNCTION, MUTAGENESIS OF TYR-257; GLU-645 AND TYR-662, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15128736; DOI=10.1074/jbc.M403777200;
Lum R., Tkach J.M., Vierling E., Glover J.R.;
"Evidence for an unfolding/threading mechanism for protein
disaggregation by Saccharomyces cerevisiae Hsp104.";
J. Biol. Chem. 279:29139-29146(2004).
[37]
MUTAGENESIS OF GLY-217; THR-499; ALA-503 AND ALA-509.
PubMed=14978213; DOI=10.1091/mbc.E02-08-0502;
Schirmer E.C., Homann O.R., Kowal A.S., Lindquist S.L.;
"Dominant gain-of-function mutations in Hsp104p reveal crucial roles
for the middle region.";
Mol. Biol. Cell 15:2061-2072(2004).
[38]
INDUCTION.
PubMed=15049822; DOI=10.1111/j.1365-2958.2003.03959.x;
Seppae L., Haenninen A.-L., Makarow M.;
"Upregulation of the Hsp104 chaperone at physiological temperature
during recovery from thermal insult.";
Mol. Microbiol. 52:217-225(2004).
[39]
FUNCTION IN PRION PROPAGATION.
PubMed=15155912; DOI=10.1126/science.1098007;
Shorter J., Lindquist S.L.;
"Hsp104 catalyzes formation and elimination of self-replicating Sup35
prion conformers.";
Science 304:1793-1797(2004).
[40]
FUNCTION.
PubMed=15843375; DOI=10.1074/jbc.M502697200;
Haslbeck M., Miess A., Stromer T., Walter S., Buchner J.;
"Disassembling protein aggregates in the yeast cytosol. The
cooperation of Hsp26 with Ssa1 and Hsp104.";
J. Biol. Chem. 280:23861-23868(2005).
[41]
FUNCTION.
PubMed=15845535; DOI=10.1074/jbc.M502854200;
Cashikar A.G., Duennwald M., Lindquist S.L.;
"A chaperone pathway in protein disaggregation. Hsp26 alters the
nature of protein aggregates to facilitate reactivation by Hsp104.";
J. Biol. Chem. 280:23869-23875(2005).
[42]
ERRATUM.
Cashikar A.G., Duennwald M., Lindquist S.L.;
J. Biol. Chem. 281:8996-8996(2006).
[43]
SUBUNIT, AND MUTAGENESIS OF LYS-218; GLU-285; LYS-620 AND GLU-687.
PubMed=16135516; DOI=10.1074/jbc.M506149200;
Boesl B., Grimminger V., Walter S.;
"Substrate binding to the molecular chaperone Hsp104 and its
regulation by nucleotides.";
J. Biol. Chem. 280:38170-38176(2005).
[44]
FUNCTION IN PRION DISASSEMBLY.
PubMed=16570324; DOI=10.1002/cbic.200500382;
Narayanan S., Walter S., Reif B.;
"Yeast prion-protein, sup35, fibril formation proceeds by addition and
substraction of oligomers.";
ChemBioChem 7:757-765(2006).
[45]
FUNCTION IN PRION DISASSEMBLY.
PubMed=16885031; DOI=10.1016/j.molcel.2006.05.042;
Shorter J., Lindquist S.L.;
"Destruction or potentiation of different prions catalyzed by similar
Hsp104 remodeling activities.";
Mol. Cell 23:425-438(2006).
[46]
SUBUNIT, ELECTRON MICROSCOPY, AND MUTAGENESIS OF ARG-334; ARG-419;
ARG-444; ARG-495; ASN-728 AND ARG-765.
PubMed=18160044; DOI=10.1016/j.cell.2007.10.047;
Wendler P., Shorter J., Plisson C., Cashikar A.G., Lindquist S.L.,
Saibil H.R.;
"Atypical AAA+ subunit packing creates an expanded cavity for
disaggregation by the protein-remodeling factor Hsp104.";
Cell 131:1366-1377(2007).
[47]
FUNCTION, AND MUTAGENESIS OF LYS-218; GLU-285; LYS-620 AND GLU-687.
PubMed=17543332; DOI=10.1016/j.jmb.2007.04.070;
Schaupp A., Marcinowski M., Grimminger V., Boesl B., Walter S.;
"Processing of proteins by the molecular chaperone Hsp104.";
J. Mol. Biol. 370:674-686(2007).
[48]
FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LEU-462; PRO-557 AND
ASP-704.
PubMed=17367387; DOI=10.1111/j.1365-2958.2007.05629.x;
Kurahashi H., Nakamura Y.;
"Channel mutations in Hsp104 hexamer distinctively affect
thermotolerance and prion-specific propagation.";
Mol. Microbiol. 63:1669-1683(2007).
[49]
FUNCTION, AND MUTAGENESIS OF LYS-218; THR-317; LYS-620 AND ASN-728.
PubMed=17259993; DOI=10.1038/nsmb1198;
Doyle S.M., Shorter J., Zolkiewski M., Hoskins J.R., Lindquist S.L.,
Wickner S.;
"Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes
protein-remodeling activity.";
Nat. Struct. Mol. Biol. 14:114-122(2007).
[50]
FUNCTION IN PRION PROPAGATION.
PubMed=17253904; DOI=10.1371/journal.pbio.0050024;
Satpute-Krishnan P., Langseth S.X., Serio T.R.;
"Hsp104-dependent remodeling of prion complexes mediates protein-only
inheritance.";
PLoS Biol. 5:251-262(2007).
[51]
INTERACTION WITH CPR7.
PubMed=18197703; DOI=10.1021/bi701714s;
Mackay R.G., Helsen C.W., Tkach J.M., Glover J.R.;
"The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a
role in oligomer assembly.";
Biochemistry 47:1918-1927(2008).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-306; THR-499
AND SER-535, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
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).
[53]
FUNCTION.
PubMed=18312264; DOI=10.1111/j.1365-2958.2008.06135.x;
Tessarz P., Mogk A., Bukau B.;
"Substrate threading through the central pore of the Hsp104 chaperone
as a common mechanism for protein disaggregation and prion
propagation.";
Mol. Microbiol. 68:87-97(2008).
[54]
SUBCELLULAR LOCATION.
PubMed=18756251; DOI=10.1038/nature07195;
Kaganovich D., Kopito R., Frydman J.;
"Misfolded proteins partition between two distinct quality control
compartments.";
Nature 454:1088-1095(2008).
[55]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-778; LYS-782 AND LYS-789.
PubMed=17973656; DOI=10.1111/j.1600-0854.2007.00666.x;
Tkach J.M., Glover J.R.;
"Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in
unstressed and heat-shocked cells.";
Traffic 9:39-56(2008).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[57]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[58]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-442, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- 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+].
{ECO:0000269|PubMed:10678178, ECO:0000269|PubMed:11073991,
ECO:0000269|PubMed:11375656, ECO:0000269|PubMed:11442834,
ECO:0000269|PubMed:12101251, ECO:0000269|PubMed:14507919,
ECO:0000269|PubMed:15128736, ECO:0000269|PubMed:15155912,
ECO:0000269|PubMed:15843375, ECO:0000269|PubMed:15845535,
ECO:0000269|PubMed:1600951, ECO:0000269|PubMed:16570324,
ECO:0000269|PubMed:16885031, ECO:0000269|PubMed:17253904,
ECO:0000269|PubMed:17259993, ECO:0000269|PubMed:17367387,
ECO:0000269|PubMed:17543332, ECO:0000269|PubMed:18312264,
ECO:0000269|PubMed:2188365, ECO:0000269|PubMed:7754373,
ECO:0000269|PubMed:7984243, ECO:0000269|PubMed:8407824,
ECO:0000269|PubMed:8643570, ECO:0000269|PubMed:9534180,
ECO:0000269|PubMed:9674429}.
-!- ENZYME REGULATION: Inhibited by micromolar concentrations of
guanidinium chloride. Inhibits the ATPase activity, but does not
dissociate the hexameric protein. {ECO:0000269|PubMed:14668331}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=170 uM for ATP (at NBD1) {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11782421, ECO:0000269|PubMed:15128736,
ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9624144};
KM=4.7 uM for ATP (at NBD2) {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11782421, ECO:0000269|PubMed:15128736,
ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9624144};
Vmax=1.25 nmol/min/ug enzyme for ATP
{ECO:0000269|PubMed:11158570, ECO:0000269|PubMed:11782421,
ECO:0000269|PubMed:15128736, ECO:0000269|PubMed:9534180,
ECO:0000269|PubMed:9624144};
-!- SUBUNIT: 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. {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11604493, ECO:0000269|PubMed:16135516,
ECO:0000269|PubMed:18160044, ECO:0000269|PubMed:18197703,
ECO:0000269|PubMed:8308017, ECO:0000269|PubMed:9534180,
ECO:0000269|PubMed:9674429}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-8050, EBI-8050;
-!- 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 extent, at a
'juxtanuclear quality control' (JUNQ) compartment, where soluble
ubiquitinated misfolded proteins accumulate.
-!- 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). {ECO:0000269|PubMed:11967066,
ECO:0000269|PubMed:15049822, ECO:0000269|PubMed:1600951,
ECO:0000269|PubMed:8308017, ECO:0000269|PubMed:8643570}.
-!- 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.
-!- DOMAIN: The C-terminal extension is involved in oligomerization.
-!- MISCELLANEOUS: Present with 32800 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M67479; AAA50477.1; -; Genomic_DNA.
EMBL; Z73131; CAA97475.1; -; Genomic_DNA.
EMBL; Z73130; CAA97474.1; -; Genomic_DNA.
EMBL; AY693002; AAT93021.1; -; Genomic_DNA.
EMBL; X97560; CAA66164.1; -; Genomic_DNA.
EMBL; BK006945; DAA09294.1; -; Genomic_DNA.
PIR; S61476; S61476.
RefSeq; NP_013074.1; NM_001181846.1.
PDB; 5KNE; EM; 5.64 A; A/B/C/D/E/F=6-857.
PDB; 5U2U; X-ray; 2.54 A; A/B/C=1-166.
PDB; 5VJH; EM; 4.00 A; A/B/C/D/E/F=1-908.
PDB; 5VY8; EM; 4.00 A; A/B/C/D/E/F=1-908.
PDB; 5VY9; EM; 4.00 A; A/B/C/D/E/F=1-908.
PDB; 5VYA; EM; 4.00 A; A/B/C/D/E/F=1-908.
PDBsum; 5KNE; -.
PDBsum; 5U2U; -.
PDBsum; 5VJH; -.
PDBsum; 5VY8; -.
PDBsum; 5VY9; -.
PDBsum; 5VYA; -.
ProteinModelPortal; P31539; -.
SMR; P31539; -.
BioGrid; 31226; 442.
DIP; DIP-2252N; -.
IntAct; P31539; 26.
MINT; MINT-530773; -.
STRING; 4932.YLL026W; -.
iPTMnet; P31539; -.
SWISS-2DPAGE; P31539; -.
MaxQB; P31539; -.
PRIDE; P31539; -.
EnsemblFungi; YLL026W; YLL026W; YLL026W.
GeneID; 850633; -.
KEGG; sce:YLL026W; -.
EuPathDB; FungiDB:YLL026W; -.
SGD; S000003949; HSP104.
GeneTree; ENSGT00390000012961; -.
HOGENOM; HOG000218211; -.
InParanoid; P31539; -.
KO; K03695; -.
OMA; TQVIRML; -.
OrthoDB; EOG092C0JLO; -.
BioCyc; YEAST:G3O-32130-MONOMER; -.
SABIO-RK; P31539; -.
PRO; PR:P31539; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0034399; C:nuclear periphery; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0072380; C:TRC complex; IDA:SGD.
GO; GO:0043531; F:ADP binding; IMP:SGD.
GO; GO:0005524; F:ATP binding; IMP:SGD.
GO; GO:0042623; F:ATPase activity, coupled; IDA:SGD.
GO; GO:0051087; F:chaperone binding; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0070370; P:cellular heat acclimation; IMP:SGD.
GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:SGD.
GO; GO:0001319; P:inheritance of oxidatively modified proteins involved in replicative cell aging; IMP:SGD.
GO; GO:0034975; P:protein folding in endoplasmic reticulum; IMP:SGD.
GO; GO:0019538; P:protein metabolic process; IEA:InterPro.
GO; GO:0043335; P:protein unfolding; IMP:SGD.
GO; GO:0035617; P:stress granule disassembly; IDA:SGD.
GO; GO:0070414; P:trehalose metabolism in response to heat stress; IMP:SGD.
Gene3D; 1.10.1780.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR019489; Clp_ATPase_C.
InterPro; IPR004176; Clp_N.
InterPro; IPR036628; Clp_N_dom_sf.
InterPro; IPR001270; ClpA/B.
InterPro; IPR018368; ClpA/B_CS1.
InterPro; IPR028299; ClpA/B_CS2.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 1.
Pfam; PF07724; AAA_2; 1.
Pfam; PF02861; Clp_N; 2.
Pfam; PF10431; ClpB_D2-small; 1.
PRINTS; PR00300; CLPPROTEASEA.
SMART; SM00382; AAA; 2.
SMART; SM01086; ClpB_D2-small; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF81923; SSF81923; 1.
PROSITE; PS00870; CLPAB_1; 1.
PROSITE; PS00871; CLPAB_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Chaperone; Coiled coil;
Complete proteome; Cytoplasm; Isopeptide bond; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Stress response;
Ubl conjugation.
CHAIN 1 908 Heat shock protein 104.
/FTId=PRO_0000191212.
NP_BIND 212 219 ATP 1. {ECO:0000255}.
NP_BIND 614 621 ATP 2. {ECO:0000255}.
REGION 167 411 NBD1.
REGION 541 731 NBD2.
REGION 905 908 Interaction surface for TPR repeats.
COILED 412 536 {ECO:0000255}.
MOTIF 773 789 Nuclear localization signal.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 499 499 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
CROSSLNK 442 442 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 620 620 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:14557538}.
MUTAGEN 184 184 D->A,D,F,N,L,Q,S: Confers resistance to
prion-curing by guanidine.
{ECO:0000269|PubMed:12105276}.
MUTAGEN 184 184 D->K,W,Y: Impairs prion propagation.
{ECO:0000269|PubMed:12105276}.
MUTAGEN 217 217 G->S: Largely reduces ATP hydrolysis.
Alters bud morphology and causes septin
mislocalization; when associated with I-
499. {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:14978213,
ECO:0000269|PubMed:9624144}.
MUTAGEN 217 217 G->V: Completely abolishes ATP
hydrolysis. {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:14978213,
ECO:0000269|PubMed:9624144}.
MUTAGEN 218 218 K->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.
{ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11442834,
ECO:0000269|PubMed:11983167,
ECO:0000269|PubMed:12101251,
ECO:0000269|PubMed:16135516,
ECO:0000269|PubMed:17259993,
ECO:0000269|PubMed:17543332,
ECO:0000269|PubMed:1896074,
ECO:0000269|PubMed:8308017,
ECO:0000269|PubMed:9624144}.
MUTAGEN 257 257 Y->A: Reduces thermotolerance 10-fold.
{ECO:0000269|PubMed:15128736}.
MUTAGEN 285 285 E->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.
{ECO:0000269|PubMed:16135516,
ECO:0000269|PubMed:17543332}.
MUTAGEN 315 315 A->T: Reduces ATP hydrolysis by 98%; when
associated with T-218.
{ECO:0000269|PubMed:11983167}.
MUTAGEN 317 317 T->A: Reduces rate of ATP hydrolysis at
NBD1 nearly 10-fold. No effect on
oligomerization.
{ECO:0000269|PubMed:11782421,
ECO:0000269|PubMed:17259993}.
MUTAGEN 334 334 R->M: Reduces ATPase activity by 80%.
Impairs oligomerization.
{ECO:0000269|PubMed:18160044}.
MUTAGEN 419 419 R->M: Reduces ATPase activity by 80%.
{ECO:0000269|PubMed:18160044}.
MUTAGEN 444 444 R->M: Reduces ATPase activity by 80%.
{ECO:0000269|PubMed:18160044}.
MUTAGEN 462 462 L->R: Impairs prion propagation, but does
not affect thermotolerance.
{ECO:0000269|PubMed:17367387}.
MUTAGEN 495 495 R->M: Increases ATPase activity 3-fold.
{ECO:0000269|PubMed:18160044}.
MUTAGEN 499 499 T->I: Reduces ATP hydrolysis by 50%.
Alters bud morphology and causes septin
mislocalization; when associated with S-
217. {ECO:0000269|PubMed:14978213}.
MUTAGEN 503 503 A->V: Increases basal level of ATPase
activity and abolishes stimulation of ATP
hydrolysis upon substrate binding.
Inhibits growth at 37 degrees Celsius.
{ECO:0000269|PubMed:11983167,
ECO:0000269|PubMed:14978213}.
MUTAGEN 509 509 A->D: Reduces thermotolerance.
{ECO:0000269|PubMed:14978213}.
MUTAGEN 557 557 P->L: Impairs prion propagation, but does
not affect thermotolerance.
{ECO:0000269|PubMed:17367387}.
MUTAGEN 619 619 G->V: Impairs oligomerization at low
protein concentrations.
{ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:9624144}.
MUTAGEN 620 620 K->T: Impairs oligomerization at low
protein concentrations. Reduces ATP
hydrolysis rate. Unable to confer
thermotolerance. Comletely abolishes
ATPase activity; when associated with T-
218. {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11442834,
ECO:0000269|PubMed:12101251,
ECO:0000269|PubMed:16135516,
ECO:0000269|PubMed:17259993,
ECO:0000269|PubMed:17543332,
ECO:0000269|PubMed:1896074,
ECO:0000269|PubMed:8308017,
ECO:0000269|PubMed:9624144}.
MUTAGEN 621 621 T->A: Reduces ATP hydrolysis, but does
not affect oligomerization.
{ECO:0000269|PubMed:11158570}.
MUTAGEN 645 645 E->K: Abolishes the ability to refold
aggregated protein in vitro and to
provide thermotolerance in vivo.
{ECO:0000269|PubMed:15128736}.
MUTAGEN 662 662 Y->A,K: Abolishes the ability to refold
aggregated protein in vitro and to
provide thermotolerance in vivo.
{ECO:0000269|PubMed:15128736}.
MUTAGEN 662 662 Y->F,W: No effect.
{ECO:0000269|PubMed:15128736}.
MUTAGEN 687 687 E->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.
{ECO:0000269|PubMed:16135516,
ECO:0000269|PubMed:17543332}.
MUTAGEN 704 704 D->N: Impairs prion propagation, but does
not affect thermotolerance.
{ECO:0000269|PubMed:17367387}.
MUTAGEN 728 728 N->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.
{ECO:0000269|PubMed:11782421,
ECO:0000269|PubMed:11983167,
ECO:0000269|PubMed:17259993,
ECO:0000269|PubMed:18160044}.
MUTAGEN 765 765 R->M: Can oligomerize in the absence of
nucleotides.
{ECO:0000269|PubMed:18160044}.
MUTAGEN 778 778 K->A: In NLS17KA; fails to concentrate in
the nucleus; when associated with A-782
and A-789. {ECO:0000269|PubMed:17973656}.
MUTAGEN 782 782 K->A: In NLS17KA; fails to concentrate in
the nucleus; when associated with A-778
and A-789. {ECO:0000269|PubMed:17973656}.
MUTAGEN 789 789 K->A: In NLS17KA; fails to concentrate in
the nucleus; when associated with A-778
and A-782. {ECO:0000269|PubMed:17973656}.
MUTAGEN 819 819 Y->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.
{ECO:0000269|PubMed:11867765}.
MUTAGEN 826 826 R->M: Reduces ATP and ADP binding at NBD2
6-fold, but does not affect ATP
hydrolysis at NBD2. Reduces catalytic
rate at NBD1.
{ECO:0000269|PubMed:11867765}.
HELIX 9 24 {ECO:0000244|PDB:5U2U}.
STRAND 28 30 {ECO:0000244|PDB:5U2U}.
HELIX 32 39 {ECO:0000244|PDB:5U2U}.
HELIX 50 57 {ECO:0000244|PDB:5U2U}.
HELIX 62 73 {ECO:0000244|PDB:5U2U}.
HELIX 90 105 {ECO:0000244|PDB:5U2U}.
STRAND 109 111 {ECO:0000244|PDB:5U2U}.
HELIX 113 120 {ECO:0000244|PDB:5U2U}.
HELIX 124 132 {ECO:0000244|PDB:5U2U}.
HELIX 137 148 {ECO:0000244|PDB:5U2U}.
SEQUENCE 908 AA; 102035 MW; 4AD0E7E3AF98E318 CRC64;
MNDQTQFTER ALTILTLAQK LASDHQHPQL QPIHILAAFI ETPEDGSVPY LQNLIEKGRY
DYDLFKKVVN RNLVRIPQQQ PAPAEITPSY ALGKVLQDAA KIQKQQKDSF IAQDHILFAL
FNDSSIQQIF KEAQVDIEAI KQQALELRGN TRIDSRGADT NTPLEYLSKY AIDMTEQARQ
GKLDPVIGRE EEIRSTIRVL ARRIKSNPCL IGEPGIGKTA IIEGVAQRII DDDVPTILQG
AKLFSLDLAA LTAGAKYKGD FEERFKGVLK EIEESKTLIV LFIDEIHMLM GNGKDDAANI
LKPALSRGQL KVIGATTNNE YRSIVEKDGA FERRFQKIEV AEPSVRQTVA ILRGLQPKYE
IHHGVRILDS ALVTAAQLAK RYLPYRRLPD SALDLVDISC AGVAVARDSK PEELDSKERQ
LQLIQVEIKA LERDEDADST TKDRLKLARQ KEASLQEELE PLRQRYNEEK HGHEELTQAK
KKLDELENKA LDAERRYDTA TAADLRYFAI PDIKKQIEKL EDQVAEEERR AGANSMIQNV
VDSDTISETA ARLTGIPVKK LSESENEKLI HMERDLSSEV VGQMDAIKAV SNAVRLSRSG
LANPRQPASF LFLGLSGSGK TELAKKVAGF LFNDEDMMIR VDCSELSEKY AVSKLLGTTA
GYVGYDEGGF LTNQLQYKPY SVLLFDEVEK AHPDVLTVML QMLDDGRITS GQGKTIDCSN
CIVIMTSNLG AEFINSQQGS KIQESTKNLV MGAVRQHFRP EFLNRISSIV IFNKLSRKAI
HKIVDIRLKE IEERFEQNDK HYKLNLTQEA KDFLAKYGYS DDMGARPLNR LIQNEILNKL
ALRILKNEIK DKETVNVVLK KGKSRDENVP EEAEECLEVL PNHEATIGAD TLGDDDNEDS
MEIDDDLD


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