HS104_YEAST
ID HS104_YEAST Reviewed; 908 AA.
AC P31539; D6VXX8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Heat shock protein 104;
DE AltName: Full=Protein aggregation-remodeling factor HSP104;
GN Name=HSP104; OrderedLocusNames=YLL026W; ORFNames=L0948;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LYS-218 AND LYS-620.
RC STRAIN=ATCC 26109 / X2180 / NCYC 826;
RX PubMed=1896074; DOI=10.1038/353270a0;
RA Parsell D.A., Sanchez Y., Stitzel J.D., Lindquist S.L.;
RT "Hsp104 is a highly conserved protein with two essential nucleotide-binding
RT sites.";
RL Nature 353:270-273(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 749-908.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046100;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT known genes, a new member of the seripauperins family and a new ABC
RT transporter homologous to the human multidrug resistance protein.";
RL Yeast 13:183-188(1997).
RN [6]
RP FUNCTION.
RX PubMed=2188365; DOI=10.1126/science.2188365;
RA Sanchez Y., Lindquist S.L.;
RT "HSP104 required for induced thermotolerance.";
RL Science 248:1112-1115(1990).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=1600951; DOI=10.1002/j.1460-2075.1992.tb05295.x;
RA Sanchez Y., Taulien J., Borkovich K.A., Lindquist S.L.;
RT "Hsp104 is required for tolerance to many forms of stress.";
RL EMBO J. 11:2357-2364(1992).
RN [8]
RP FUNCTION.
RX PubMed=8407824; DOI=10.1128/jb.175.20.6484-6491.1993;
RA Sanchez Y., Parsell D.A., Taulien J., Vogel J.L., Craig E.A.,
RA Lindquist S.L.;
RT "Genetic evidence for a functional relationship between Hsp104 and Hsp70.";
RL J. Bacteriol. 175:6484-6491(1993).
RN [9]
RP INDUCTION, MUTAGENESIS OF LYS-218 AND LYS-620, SUBUNIT, AND ELECTRON
RP MICROSCOPY.
RX PubMed=8308017; DOI=10.1016/s0021-9258(17)41804-7;
RA Parsell D.A., Kowal A.S., Lindquist S.L.;
RT "Saccharomyces cerevisiae Hsp104 protein. Purification and characterization
RT of ATP-induced structural changes.";
RL J. Biol. Chem. 269:4480-4487(1994).
RN [10]
RP FUNCTION.
RX PubMed=7984243; DOI=10.1038/372475a0;
RA Parsell D.A., Kowal A.S., Singer M.A., Lindquist S.L.;
RT "Protein disaggregation mediated by heat-shock protein Hsp104.";
RL Nature 372:475-478(1994).
RN [11]
RP FUNCTION IN PRION MAINTENANCE.
RX PubMed=7754373; DOI=10.1126/science.7754373;
RA Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G., Liebman S.W.;
RT "Role of the chaperone protein Hsp104 in propagation of the yeast prion-
RT like factor [psi+].";
RL Science 268:880-884(1995).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=8643570; DOI=10.1073/pnas.93.11.5301;
RA Lindquist S.L., Kim G.;
RT "Heat-shock protein 104 expression is sufficient for thermotolerance in
RT yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5301-5306(1996).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=9703962; DOI=10.1006/bbrc.1998.9008;
RA Fujita K., Kawai R., Iwahashi H., Komatsu Y.;
RT "Hsp104 responds to heat and oxidative stress with different intracellular
RT localization in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 248:542-547(1998).
RN [14]
RP FUNCTION, AND INTERACTION WITH YDJ1.
RX PubMed=9674429; DOI=10.1016/s0092-8674(00)81223-4;
RA Glover J.R., Lindquist S.L.;
RT "Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously
RT aggregated proteins.";
RL Cell 94:73-82(1998).
RN [15]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-217; LYS-218; GLY-619
RP AND LYS-620.
RX PubMed=9624144; DOI=10.1074/jbc.273.25.15546;
RA Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S.L.;
RT "The ATPase activity of Hsp104, effects of environmental conditions and
RT mutations.";
RL J. Biol. Chem. 273:15546-15552(1998).
RN [16]
RP ERRATUM OF PUBMED:9624144.
RA Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S.L.;
RL J. Biol. Chem. 273:19922-19922(1998).
RN [17]
RP FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9534180; DOI=10.1016/s0076-6879(98)90036-2;
RA Schirmer E.C., Lindquist S.L.;
RT "Purification and properties of Hsp104 from yeast.";
RL Methods Enzymol. 290:430-444(1998).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=10467108; DOI=10.1054/csac.1999.0076;
RA Kawai R., Fujita K., Iwahashi H., Komatsu Y.;
RT "Direct evidence for the intracellular localization of Hsp104 in
RT Saccharomyces cerevisiae by immunoelectron microscopy.";
RL Cell Stress Chaperones 4:46-53(1999).
RN [19]
RP FUNCTION IN PRION PROPAGATION.
RX PubMed=10678178; DOI=10.1016/s1097-2765(00)80412-8;
RA Sondheimer N., Lindquist S.L.;
RT "Rnq1: an epigenetic modifier of protein function in yeast.";
RL Mol. Cell 5:163-172(2000).
RN [20]
RP FUNCTION IN PRION PROPAGATION.
RX PubMed=11073991; DOI=10.1128/mcb.20.23.8916-8922.2000;
RA Moriyama H., Edskes H.K., Wickner R.B.;
RT "[URE3] prion propagation in Saccharomyces cerevisiae: requirement for
RT chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.";
RL Mol. Cell. Biol. 20:8916-8922(2000).
RN [21]
RP FUNCTION IN PRION PROPAGATION.
RX PubMed=11375656; DOI=10.1007/s002840010251;
RA Jung G., Masison D.C.;
RT "Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible
RT explanation for its effect in curing yeast prions.";
RL Curr. Microbiol. 43:7-10(2001).
RN [22]
RP INTERACTION WITH CNS1; CPR7 AND STI1.
RX PubMed=11604493; DOI=10.1128/mcb.21.22.7569-7575.2001;
RA Abbas-Terki T., Donze O., Briand P.-A., Picard D.;
RT "Hsp104 interacts with Hsp90 cochaperones in respiring yeast.";
RL Mol. Cell. Biol. 21:7569-7575(2001).
RN [23]
RP FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LYS-218 AND LYS-620.
RX PubMed=11442834; DOI=10.1046/j.1365-2958.2001.02478.x;
RA Ferreira P.C., Ness F., Edwards S.R., Cox B.S., Tuite M.F.;
RT "The elimination of the yeast [PSI+] prion by guanidine hydrochloride is
RT the result of Hsp104 inactivation.";
RL Mol. Microbiol. 40:1357-1369(2001).
RN [24]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF GLY-217;
RP LYS-218; GLY-619; LYS-620 AND THR-621.
RX PubMed=11158570; DOI=10.1073/pnas.98.3.914;
RA Schirmer E.C., Ware D.M., Queitsch C., Kowal A.S., Lindquist S.L.;
RT "Subunit interactions influence the biochemical and biological properties
RT of Hsp104.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:914-919(2001).
RN [25]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF THR-317 AND ASN-728.
RX PubMed=11782421; DOI=10.1093/emboj/21.1.12;
RA Hattendorf D.A., Lindquist S.L.;
RT "Cooperative kinetics of both Hsp104 ATPase domains and interdomain
RT communication revealed by AAA sensor-1 mutants.";
RL EMBO J. 21:12-21(2002).
RN [26]
RP SUBSTRATE-BINDING, AND MUTAGENESIS OF LYS-218; ALA-315; ALA-503 AND
RP ASN-728.
RX PubMed=11983167; DOI=10.1016/s1097-2765(02)00499-9;
RA Cashikar A.G., Schirmer E.C., Hattendorf D.A., Glover J.R.,
RA Ramakrishnan M.S., Ware D.M., Lindquist S.L.;
RT "Defining a pathway of communication from the C-terminal peptide binding
RT domain to the N-terminal ATPase domain in a AAA protein.";
RL Mol. Cell 9:751-760(2002).
RN [27]
RP FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LYS-218 AND LYS-620.
RX PubMed=12101251; DOI=10.1128/mcb.22.15.5593-5605.2002;
RA Ness F., Ferreira P.C., Cox B.S., Tuite M.F.;
RT "Guanidine hydrochloride inhibits the generation of prion 'seeds' but not
RT prion protein aggregation in yeast.";
RL Mol. Cell. Biol. 22:5593-5605(2002).
RN [28]
RP INDUCTION.
RX PubMed=11967066; DOI=10.1046/j.1365-2958.2002.02860.x;
RA Grably M.R., Stanhill A., Tell O., Engelberg D.;
RT "HSF and Msn2/4p can exclusively or cooperatively activate the yeast HSP104
RT gene.";
RL Mol. Microbiol. 44:21-35(2002).
RN [29]
RP MUTAGENESIS OF TYR-819 AND ARG-826, AND ATP-BINDING.
RX PubMed=11867765; DOI=10.1073/pnas.261693199;
RA Hattendorf D.A., Lindquist S.L.;
RT "Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of
RT Hsp104 with a site-specific fluorescent probe of nucleotide binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2732-2737(2002).
RN [30]
RP MUTAGENESIS OF ASP-184.
RX PubMed=12105276; DOI=10.1073/pnas.152333299;
RA Jung G., Jones G., Masison D.C.;
RT "Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-
RT curing by guanidine, prion propagation, and thermotolerance.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9936-9941(2002).
RN [31]
RP FUNCTION IN PRION FRAGMENTATION.
RX PubMed=14507919; DOI=10.1074/jbc.m307996200;
RA Kryndushkin D.S., Alexandrov I.M., Ter-Avanesyan M.D., Kushnirov V.V.;
RT "Yeast [PSI+] prion aggregates are formed by small Sup35 polymers
RT fragmented by Hsp104.";
RL J. Biol. Chem. 278:49636-49643(2003).
RN [32]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [33]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [34]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-620, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [35]
RP ACTIVITY REGULATION.
RX PubMed=14668331; DOI=10.1074/jbc.m312403200;
RA Grimminger V., Richter K., Imhof A., Buchner J., Walter S.;
RT "The prion curing agent guanidinium chloride specifically inhibits ATP
RT hydrolysis by Hsp104.";
RL J. Biol. Chem. 279:7378-7383(2004).
RN [36]
RP FUNCTION, MUTAGENESIS OF TYR-257; GLU-645 AND TYR-662, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15128736; DOI=10.1074/jbc.m403777200;
RA Lum R., Tkach J.M., Vierling E., Glover J.R.;
RT "Evidence for an unfolding/threading mechanism for protein disaggregation
RT by Saccharomyces cerevisiae Hsp104.";
RL J. Biol. Chem. 279:29139-29146(2004).
RN [37]
RP MUTAGENESIS OF GLY-217; THR-499; ALA-503 AND ALA-509.
RX PubMed=14978213; DOI=10.1091/mbc.e02-08-0502;
RA Schirmer E.C., Homann O.R., Kowal A.S., Lindquist S.L.;
RT "Dominant gain-of-function mutations in Hsp104p reveal crucial roles for
RT the middle region.";
RL Mol. Biol. Cell 15:2061-2072(2004).
RN [38]
RP INDUCTION.
RX PubMed=15049822; DOI=10.1111/j.1365-2958.2003.03959.x;
RA Seppae L., Haenninen A.-L., Makarow M.;
RT "Upregulation of the Hsp104 chaperone at physiological temperature during
RT recovery from thermal insult.";
RL Mol. Microbiol. 52:217-225(2004).
RN [39]
RP FUNCTION IN PRION PROPAGATION.
RX PubMed=15155912; DOI=10.1126/science.1098007;
RA Shorter J., Lindquist S.L.;
RT "Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion
RT conformers.";
RL Science 304:1793-1797(2004).
RN [40]
RP FUNCTION.
RX PubMed=15843375; DOI=10.1074/jbc.m502697200;
RA Haslbeck M., Miess A., Stromer T., Walter S., Buchner J.;
RT "Disassembling protein aggregates in the yeast cytosol. The cooperation of
RT Hsp26 with Ssa1 and Hsp104.";
RL J. Biol. Chem. 280:23861-23868(2005).
RN [41]
RP FUNCTION.
RX PubMed=15845535; DOI=10.1074/jbc.m502854200;
RA Cashikar A.G., Duennwald M., Lindquist S.L.;
RT "A chaperone pathway in protein disaggregation. Hsp26 alters the nature of
RT protein aggregates to facilitate reactivation by Hsp104.";
RL J. Biol. Chem. 280:23869-23875(2005).
RN [42]
RP ERRATUM OF PUBMED:15845535.
RA Cashikar A.G., Duennwald M., Lindquist S.L.;
RL J. Biol. Chem. 281:8996-8996(2006).
RN [43]
RP SUBUNIT, AND MUTAGENESIS OF LYS-218; GLU-285; LYS-620 AND GLU-687.
RX PubMed=16135516; DOI=10.1074/jbc.m506149200;
RA Boesl B., Grimminger V., Walter S.;
RT "Substrate binding to the molecular chaperone Hsp104 and its regulation by
RT nucleotides.";
RL J. Biol. Chem. 280:38170-38176(2005).
RN [44]
RP FUNCTION IN PRION DISASSEMBLY.
RX PubMed=16570324; DOI=10.1002/cbic.200500382;
RA Narayanan S., Walter S., Reif B.;
RT "Yeast prion-protein, sup35, fibril formation proceeds by addition and
RT substraction of oligomers.";
RL ChemBioChem 7:757-765(2006).
RN [45]
RP FUNCTION IN PRION DISASSEMBLY.
RX PubMed=16885031; DOI=10.1016/j.molcel.2006.05.042;
RA Shorter J., Lindquist S.L.;
RT "Destruction or potentiation of different prions catalyzed by similar
RT Hsp104 remodeling activities.";
RL Mol. Cell 23:425-438(2006).
RN [46]
RP SUBUNIT, ELECTRON MICROSCOPY, AND MUTAGENESIS OF ARG-334; ARG-419; ARG-444;
RP ARG-495; ASN-728 AND ARG-765.
RX PubMed=18160044; DOI=10.1016/j.cell.2007.10.047;
RA Wendler P., Shorter J., Plisson C., Cashikar A.G., Lindquist S.L.,
RA Saibil H.R.;
RT "Atypical AAA+ subunit packing creates an expanded cavity for
RT disaggregation by the protein-remodeling factor Hsp104.";
RL Cell 131:1366-1377(2007).
RN [47]
RP FUNCTION, AND MUTAGENESIS OF LYS-218; GLU-285; LYS-620 AND GLU-687.
RX PubMed=17543332; DOI=10.1016/j.jmb.2007.04.070;
RA Schaupp A., Marcinowski M., Grimminger V., Boesl B., Walter S.;
RT "Processing of proteins by the molecular chaperone Hsp104.";
RL J. Mol. Biol. 370:674-686(2007).
RN [48]
RP FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LEU-462; PRO-557 AND
RP ASP-704.
RX PubMed=17367387; DOI=10.1111/j.1365-2958.2007.05629.x;
RA Kurahashi H., Nakamura Y.;
RT "Channel mutations in Hsp104 hexamer distinctively affect thermotolerance
RT and prion-specific propagation.";
RL Mol. Microbiol. 63:1669-1683(2007).
RN [49]
RP FUNCTION, AND MUTAGENESIS OF LYS-218; THR-317; LYS-620 AND ASN-728.
RX PubMed=17259993; DOI=10.1038/nsmb1198;
RA Doyle S.M., Shorter J., Zolkiewski M., Hoskins J.R., Lindquist S.L.,
RA Wickner S.;
RT "Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes
RT protein-remodeling activity.";
RL Nat. Struct. Mol. Biol. 14:114-122(2007).
RN [50]
RP FUNCTION IN PRION PROPAGATION.
RX PubMed=17253904; DOI=10.1371/journal.pbio.0050024;
RA Satpute-Krishnan P., Langseth S.X., Serio T.R.;
RT "Hsp104-dependent remodeling of prion complexes mediates protein-only
RT inheritance.";
RL PLoS Biol. 5:251-262(2007).
RN [51]
RP INTERACTION WITH CPR7.
RX PubMed=18197703; DOI=10.1021/bi701714s;
RA Mackay R.G., Helsen C.W., Tkach J.M., Glover J.R.;
RT "The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role
RT in oligomer assembly.";
RL Biochemistry 47:1918-1927(2008).
RN [52]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-306; THR-499 AND
RP SER-535, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [53]
RP FUNCTION.
RX PubMed=18312264; DOI=10.1111/j.1365-2958.2008.06135.x;
RA Tessarz P., Mogk A., Bukau B.;
RT "Substrate threading through the central pore of the Hsp104 chaperone as a
RT common mechanism for protein disaggregation and prion propagation.";
RL Mol. Microbiol. 68:87-97(2008).
RN [54]
RP SUBCELLULAR LOCATION.
RX PubMed=18756251; DOI=10.1038/nature07195;
RA Kaganovich D., Kopito R., Frydman J.;
RT "Misfolded proteins partition between two distinct quality control
RT compartments.";
RL Nature 454:1088-1095(2008).
RN [55]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-778; LYS-782 AND LYS-789.
RX PubMed=17973656; DOI=10.1111/j.1600-0854.2007.00666.x;
RA Tkach J.M., Glover J.R.;
RT "Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in
RT unstressed and heat-shocked cells.";
RL Traffic 9:39-56(2008).
RN [56]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [57]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [58]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-442, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and
CC small Hsps (HSP26), for the dissociation, resolubilization and
CC refolding of aggregates of damaged proteins after heat or other
CC environmental stresses. Extracts proteins from aggregates by unfolding
CC and threading them in an ATP-dependent process through the axial
CC channel of the protein hexamer, after which they can be refolded by
CC components of the Hsp70/Hsp40 chaperone system. Substrate binding is
CC ATP-dependent, and release of bound polypeptide is triggered by ATP
CC hydrolysis. Also responsible for the maintenance of prions by
CC dissociating prion fibrils into smaller oligomers, thereby producing
CC transmissible seeds that can infect daughter cells during mitosis and
CC meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+],
CC [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of
CC [PSI+]. {ECO:0000269|PubMed:10678178, ECO:0000269|PubMed:11073991,
CC ECO:0000269|PubMed:11375656, ECO:0000269|PubMed:11442834,
CC ECO:0000269|PubMed:12101251, ECO:0000269|PubMed:14507919,
CC ECO:0000269|PubMed:15128736, ECO:0000269|PubMed:15155912,
CC ECO:0000269|PubMed:15843375, ECO:0000269|PubMed:15845535,
CC ECO:0000269|PubMed:1600951, ECO:0000269|PubMed:16570324,
CC ECO:0000269|PubMed:16885031, ECO:0000269|PubMed:17253904,
CC ECO:0000269|PubMed:17259993, ECO:0000269|PubMed:17367387,
CC ECO:0000269|PubMed:17543332, ECO:0000269|PubMed:18312264,
CC ECO:0000269|PubMed:2188365, ECO:0000269|PubMed:7754373,
CC ECO:0000269|PubMed:7984243, ECO:0000269|PubMed:8407824,
CC ECO:0000269|PubMed:8643570, ECO:0000269|PubMed:9534180,
CC ECO:0000269|PubMed:9674429}.
CC -!- ACTIVITY REGULATION: Inhibited by micromolar concentrations of
CC guanidinium chloride. Inhibits the ATPase activity, but does not
CC dissociate the hexameric protein. {ECO:0000269|PubMed:14668331}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=170 uM for ATP (at NBD1) {ECO:0000269|PubMed:11158570,
CC ECO:0000269|PubMed:11782421, ECO:0000269|PubMed:15128736,
CC ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9624144};
CC KM=4.7 uM for ATP (at NBD2) {ECO:0000269|PubMed:11158570,
CC ECO:0000269|PubMed:11782421, ECO:0000269|PubMed:15128736,
CC ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9624144};
CC Vmax=1.25 nmol/min/ug enzyme for ATP {ECO:0000269|PubMed:11158570,
CC ECO:0000269|PubMed:11782421, ECO:0000269|PubMed:15128736,
CC ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9624144};
CC -!- SUBUNIT: Homohexamer, forming a ring with a central pore. The hexamer
CC is stabilized by high protein concentrations and by ADP or ATP.
CC Oligomerization influences ATP hydrolysis activity at NBD2. Interacts
CC with YDJ1. Interacts (via C-terminal DDLD tetrapeptide) with CNS1, CPR7
CC and STI1 (via TPR repeats); under respiratory growth conditions.
CC {ECO:0000269|PubMed:11158570, ECO:0000269|PubMed:11604493,
CC ECO:0000269|PubMed:16135516, ECO:0000269|PubMed:18160044,
CC ECO:0000269|PubMed:18197703, ECO:0000269|PubMed:8308017,
CC ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9674429}.
CC -!- INTERACTION:
CC P31539; P31539: HSP104; NbExp=3; IntAct=EBI-8050, EBI-8050;
CC P31539; Q12285: MDY2; NbExp=2; IntAct=EBI-8050, EBI-34904;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC cytoplasm and the nucleus in an importin KAP95- and KAP121-dependent
CC and an exportin XPO1-dependent manner. Accumulation in the nucleus is
CC enhanced by severe heat shock. In the cytoplasm, concentrates on a
CC perivacuolar compartment, the 'insoluble protein deposit' (IPOD), in
CC which terminally aggregated proteins are sequestered. It is also found,
CC to a lesser extent, at a 'juxtanuclear quality control' (JUNQ)
CC compartment, where soluble ubiquitinated misfolded proteins accumulate.
CC -!- INDUCTION: By heat stress dependent on the heat shock transcription
CC factor HSF1 and the general stress transcription factors MSN2 and MSN4.
CC Expressed at a higher level in respiring cells than in fermenting
CC cells. Expressed in stationary phase cells and spores (at protein
CC level). {ECO:0000269|PubMed:11967066, ECO:0000269|PubMed:15049822,
CC ECO:0000269|PubMed:1600951, ECO:0000269|PubMed:8308017,
CC ECO:0000269|PubMed:8643570}.
CC -!- DOMAIN: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per
CC monomer, a low-affinity, high-turnover site (NBD1) and a high-affinity
CC site (NBD2) with a 300-fold slower rate of hydrolysis. There is
CC allosteric regulation between the 2 sites. ATP binding to NBD1 triggers
CC binding of polypeptides and stimulates ATP hydrolysis at NBD2.
CC Nucleotide binding to NBD2 is crucial for oligomerization.
CC -!- DOMAIN: The C-terminal extension is involved in oligomerization.
CC -!- MISCELLANEOUS: Present with 32800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; M67479; AAA50477.1; -; Genomic_DNA.
DR EMBL; Z73131; CAA97475.1; -; Genomic_DNA.
DR EMBL; Z73130; CAA97474.1; -; Genomic_DNA.
DR EMBL; AY693002; AAT93021.1; -; Genomic_DNA.
DR EMBL; X97560; CAA66164.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09294.1; -; Genomic_DNA.
DR PIR; S61476; S61476.
DR RefSeq; NP_013074.1; NM_001181846.1.
DR PDB; 5KNE; EM; 5.64 A; A/B/C/D/E/F=6-857.
DR PDB; 5U2U; X-ray; 2.54 A; A/B/C=1-166.
DR PDB; 5VJH; EM; 4.00 A; A/B/C/D/E/F=1-908.
DR PDB; 5VY8; EM; 4.00 A; A/B/C/D/E/F=1-908.
DR PDB; 5VY9; EM; 4.00 A; A/B/C/D/E/F=1-908.
DR PDB; 5VYA; EM; 4.00 A; A/B/C/D/E/F=1-908.
DR PDB; 5WBW; X-ray; 2.60 A; A/B/D=4-356.
DR PDB; 6AHF; EM; 6.78 A; A/B/C/D/E/F=1-908.
DR PDB; 6AMN; X-ray; 2.82 A; A=4-352.
DR PDB; 6N8T; EM; 7.70 A; A/B/C/D/E/F=6-884.
DR PDB; 6N8V; EM; 5.64 A; A/B/C/D/E/F=6-884.
DR PDB; 6N8Z; EM; 9.30 A; A/B/C/D/E/F=6-884.
DR PDBsum; 5KNE; -.
DR PDBsum; 5U2U; -.
DR PDBsum; 5VJH; -.
DR PDBsum; 5VY8; -.
DR PDBsum; 5VY9; -.
DR PDBsum; 5VYA; -.
DR PDBsum; 5WBW; -.
DR PDBsum; 6AHF; -.
DR PDBsum; 6AMN; -.
DR PDBsum; 6N8T; -.
DR PDBsum; 6N8V; -.
DR PDBsum; 6N8Z; -.
DR AlphaFoldDB; P31539; -.
DR SMR; P31539; -.
DR BioGRID; 31226; 489.
DR ComplexPortal; CPX-1861; GET4-GET5 transmembrane domain recognition complex.
DR DIP; DIP-2252N; -.
DR IntAct; P31539; 28.
DR MINT; P31539; -.
DR STRING; 4932.YLL026W; -.
DR CarbonylDB; P31539; -.
DR iPTMnet; P31539; -.
DR SWISS-2DPAGE; P31539; -.
DR MaxQB; P31539; -.
DR PaxDb; P31539; -.
DR PRIDE; P31539; -.
DR EnsemblFungi; YLL026W_mRNA; YLL026W; YLL026W.
DR GeneID; 850633; -.
DR KEGG; sce:YLL026W; -.
DR SGD; S000003949; HSP104.
DR VEuPathDB; FungiDB:YLL026W; -.
DR eggNOG; KOG1051; Eukaryota.
DR GeneTree; ENSGT00960000189194; -.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; P31539; -.
DR OMA; ERMKAVM; -.
DR BioCyc; YEAST:G3O-32130-MON; -.
DR SABIO-RK; P31539; -.
DR PRO; PR:P31539; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P31539; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0072380; C:TRC complex; IDA:SGD.
DR GO; GO:0043531; F:ADP binding; IMP:SGD.
DR GO; GO:0005524; F:ATP binding; IMP:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:SGD.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:SGD.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0043335; P:protein unfolding; IMP:SGD.
DR GO; GO:0035617; P:stress granule disassembly; IDA:SGD.
DR GO; GO:0070414; P:trehalose metabolism in response to heat stress; IMP:SGD.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Stress response; Ubl conjugation.
FT CHAIN 1..908
FT /note="Heat shock protein 104"
FT /id="PRO_0000191212"
FT DOMAIN 4..150
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 7..76
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 88..150
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 167..411
FT /note="NBD1"
FT REGION 541..731
FT /note="NBD2"
FT REGION 883..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..908
FT /note="Interaction surface for TPR repeats"
FT COILED 412..536
FT /evidence="ECO:0000255"
FT MOTIF 773..789
FT /note="Nuclear localization signal"
FT COMPBIAS 891..908
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 614..621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:14557538"
FT MUTAGEN 184
FT /note="D->A,D,F,N,L,Q,S: Confers resistance to prion-curing
FT by guanidine."
FT /evidence="ECO:0000269|PubMed:12105276"
FT MUTAGEN 184
FT /note="D->K,W,Y: Impairs prion propagation."
FT /evidence="ECO:0000269|PubMed:12105276"
FT MUTAGEN 217
FT /note="G->S: Largely reduces ATP hydrolysis. Alters bud
FT morphology and causes septin mislocalization; when
FT associated with I-499."
FT /evidence="ECO:0000269|PubMed:11158570,
FT ECO:0000269|PubMed:14978213, ECO:0000269|PubMed:9624144"
FT MUTAGEN 217
FT /note="G->V: Completely abolishes ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:11158570,
FT ECO:0000269|PubMed:14978213, ECO:0000269|PubMed:9624144"
FT MUTAGEN 218
FT /note="K->T: Abolishes substrate binding. Unable to confer
FT thermotolerance. Reduces ATP hydrolysis by 98%; when
FT associated with T-315. Completely abolishes ATPase
FT activity; when associated with T-620."
FT /evidence="ECO:0000269|PubMed:11158570,
FT ECO:0000269|PubMed:11442834, ECO:0000269|PubMed:11983167,
FT ECO:0000269|PubMed:12101251, ECO:0000269|PubMed:16135516,
FT ECO:0000269|PubMed:17259993, ECO:0000269|PubMed:17543332,
FT ECO:0000269|PubMed:1896074, ECO:0000269|PubMed:8308017,
FT ECO:0000269|PubMed:9624144"
FT MUTAGEN 257
FT /note="Y->A: Reduces thermotolerance 10-fold."
FT /evidence="ECO:0000269|PubMed:15128736"
FT MUTAGEN 285
FT /note="E->Q: In HSP104(TRAP); completely abolishes ATP
FT hydrolysis, but does not affect nucleotide binding, thus
FT keeping HSP104 in an ATP-bound state; when associated with
FT Q-687."
FT /evidence="ECO:0000269|PubMed:16135516,
FT ECO:0000269|PubMed:17543332"
FT MUTAGEN 315
FT /note="A->T: Reduces ATP hydrolysis by 98%; when associated
FT with T-218."
FT /evidence="ECO:0000269|PubMed:11983167"
FT MUTAGEN 317
FT /note="T->A: Reduces rate of ATP hydrolysis at NBD1 nearly
FT 10-fold. No effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:11782421,
FT ECO:0000269|PubMed:17259993"
FT MUTAGEN 334
FT /note="R->M: Reduces ATPase activity by 80%. Impairs
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:18160044"
FT MUTAGEN 419
FT /note="R->M: Reduces ATPase activity by 80%."
FT /evidence="ECO:0000269|PubMed:18160044"
FT MUTAGEN 444
FT /note="R->M: Reduces ATPase activity by 80%."
FT /evidence="ECO:0000269|PubMed:18160044"
FT MUTAGEN 462
FT /note="L->R: Impairs prion propagation, but does not affect
FT thermotolerance."
FT /evidence="ECO:0000269|PubMed:17367387"
FT MUTAGEN 495
FT /note="R->M: Increases ATPase activity 3-fold."
FT /evidence="ECO:0000269|PubMed:18160044"
FT MUTAGEN 499
FT /note="T->I: Reduces ATP hydrolysis by 50%. Alters bud
FT morphology and causes septin mislocalization; when
FT associated with S-217."
FT /evidence="ECO:0000269|PubMed:14978213"
FT MUTAGEN 503
FT /note="A->V: Increases basal level of ATPase activity and
FT abolishes stimulation of ATP hydrolysis upon substrate
FT binding. Inhibits growth at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11983167,
FT ECO:0000269|PubMed:14978213"
FT MUTAGEN 509
FT /note="A->D: Reduces thermotolerance."
FT /evidence="ECO:0000269|PubMed:14978213"
FT MUTAGEN 557
FT /note="P->L: Impairs prion propagation, but does not affect
FT thermotolerance."
FT /evidence="ECO:0000269|PubMed:17367387"
FT MUTAGEN 619
FT /note="G->V: Impairs oligomerization at low protein
FT concentrations."
FT /evidence="ECO:0000269|PubMed:11158570,
FT ECO:0000269|PubMed:9624144"
FT MUTAGEN 620
FT /note="K->T: Impairs oligomerization at low protein
FT concentrations. Reduces ATP hydrolysis rate. Unable to
FT confer thermotolerance. Completely abolishes ATPase
FT activity; when associated with T-218."
FT /evidence="ECO:0000269|PubMed:11158570,
FT ECO:0000269|PubMed:11442834, ECO:0000269|PubMed:12101251,
FT ECO:0000269|PubMed:16135516, ECO:0000269|PubMed:17259993,
FT ECO:0000269|PubMed:17543332, ECO:0000269|PubMed:1896074,
FT ECO:0000269|PubMed:8308017, ECO:0000269|PubMed:9624144"
FT MUTAGEN 621
FT /note="T->A: Reduces ATP hydrolysis, but does not affect
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:11158570"
FT MUTAGEN 645
FT /note="E->K: Abolishes the ability to refold aggregated
FT protein in vitro and to provide thermotolerance in vivo."
FT /evidence="ECO:0000269|PubMed:15128736"
FT MUTAGEN 662
FT /note="Y->A,K: Abolishes the ability to refold aggregated
FT protein in vitro and to provide thermotolerance in vivo."
FT /evidence="ECO:0000269|PubMed:15128736"
FT MUTAGEN 662
FT /note="Y->F,W: No effect."
FT /evidence="ECO:0000269|PubMed:15128736"
FT MUTAGEN 687
FT /note="E->Q: In HSP104(TRAP); completely abolishes ATP
FT hydrolysis, but does not affect nucleotide binding, thus
FT keeping HSP104 in an ATP-bound state; when associated with
FT Q-285."
FT /evidence="ECO:0000269|PubMed:16135516,
FT ECO:0000269|PubMed:17543332"
FT MUTAGEN 704
FT /note="D->N: Impairs prion propagation, but does not affect
FT thermotolerance."
FT /evidence="ECO:0000269|PubMed:17367387"
FT MUTAGEN 728
FT /note="N->A: Almost completely abolishes ATP hydrolysis at
FT NBD2, but does not affect nucleotide binding, thus keeping
FT NBD2 in an ATP-bound state. Reduces stimulation of ATP
FT hydrolysis upon substrate binding."
FT /evidence="ECO:0000269|PubMed:11782421,
FT ECO:0000269|PubMed:11983167, ECO:0000269|PubMed:17259993,
FT ECO:0000269|PubMed:18160044"
FT MUTAGEN 765
FT /note="R->M: Can oligomerize in the absence of
FT nucleotides."
FT /evidence="ECO:0000269|PubMed:18160044"
FT MUTAGEN 778
FT /note="K->A: In NLS17KA; fails to concentrate in the
FT nucleus; when associated with A-782 and A-789."
FT /evidence="ECO:0000269|PubMed:17973656"
FT MUTAGEN 782
FT /note="K->A: In NLS17KA; fails to concentrate in the
FT nucleus; when associated with A-778 and A-789."
FT /evidence="ECO:0000269|PubMed:17973656"
FT MUTAGEN 789
FT /note="K->A: In NLS17KA; fails to concentrate in the
FT nucleus; when associated with A-778 and A-782."
FT /evidence="ECO:0000269|PubMed:17973656"
FT MUTAGEN 819
FT /note="Y->W: Site-specific fluorescent probe in an
FT otherwise Trp-less HSP104. Fluorescence of this Trp changes
FT in response to ATP and ADP binding at NBD2. Has no effect
FT on ATP hydrolysis or protein stability."
FT /evidence="ECO:0000269|PubMed:11867765"
FT MUTAGEN 826
FT /note="R->M: Reduces ATP and ADP binding at NBD2 6-fold,
FT but does not affect ATP hydrolysis at NBD2. Reduces
FT catalytic rate at NBD1."
FT /evidence="ECO:0000269|PubMed:11867765"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:5U2U"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5U2U"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:5U2U"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:5U2U"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:5U2U"
FT HELIX 90..105
FT /evidence="ECO:0007829|PDB:5U2U"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5U2U"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:5U2U"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:5U2U"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:5U2U"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:5WBW"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:5WBW"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5WBW"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:5WBW"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 260..273
FT /evidence="ECO:0007829|PDB:5WBW"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:5WBW"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:5WBW"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:5WBW"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:5WBW"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:5WBW"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:5WBW"
FT TURN 351..355
FT /evidence="ECO:0007829|PDB:5WBW"
SQ 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
