HSP78_YEAST
ID HSP78_YEAST Reviewed; 811 AA.
AC P33416; D6VSN8; Q12137;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Heat shock protein 78, mitochondrial;
DE Flags: Precursor;
GN Name=HSP78; OrderedLocusNames=YDR258C; ORFNames=YD9320A.08C;
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], SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=8413229; DOI=10.1128/mcb.13.10.6304-6313.1993;
RA Leonhardt S.A., Fearon K., Danese P.N., Mason T.L.;
RT "HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family
RT of ATP-dependent proteases.";
RL Mol. Cell. Biol. 13:6304-6313(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 PROTEIN SEQUENCE OF 85-90, AND FUNCTION.
RX PubMed=11231020; DOI=10.1016/s0014-5793(00)02423-6;
RA Krzewska J., Langer T., Liberek K.;
RT "Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces
RT cerevisiae, cooperates with Hsp70 in protein refolding.";
RL FEBS Lett. 489:92-96(2001).
RN [5]
RP FUNCTION.
RX PubMed=7628444; DOI=10.1002/j.1460-2075.1995.tb07349.x;
RA Schmitt M., Neupert W., Langer T.;
RT "Hsp78, a Clp homologue within mitochondria, can substitute for chaperone
RT functions of mt-hsp70.";
RL EMBO J. 14:3434-3444(1995).
RN [6]
RP FUNCTION.
RX PubMed=7500331; DOI=10.1006/jmbi.1995.0636;
RA Moczko M., Schoenfisch B., Voos W., Pfanner N., Rassow J.;
RT "The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in
RT maintenance of mitochondrial function.";
RL J. Mol. Biol. 254:538-543(1995).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8830768; DOI=10.1083/jcb.134.6.1375;
RA Schmitt M., Neupert W., Langer T.;
RT "The molecular chaperone Hsp78 confers compartment-specific thermotolerance
RT to mitochondria.";
RL J. Cell Biol. 134:1375-1386(1996).
RN [8]
RP FUNCTION, SUBUNIT, ELECTRON MICROSCOPY, AND MUTAGENESIS OF LYS-149 AND
RP LYS-547.
RX PubMed=11734006; DOI=10.1006/jmbi.2001.5190;
RA Krzewska J., Konopa G., Liberek K.;
RT "Importance of two ATP-binding sites for oligomerization, ATPase activity
RT and chaperone function of mitochondrial Hsp78 protein.";
RL J. Mol. Biol. 314:901-910(2001).
RN [9]
RP FUNCTION.
RX PubMed=12023279; DOI=10.1074/jbc.m201756200;
RA Germaniuk A., Liberek K., Marszalek J.;
RT "A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis
RT following thermal inactivation of Mip1p polymerase.";
RL J. Biol. Chem. 277:27801-27808(2002).
RN [10]
RP FUNCTION IN PROTEIN DEGRADATION.
RX PubMed=12237310; DOI=10.1074/jbc.m207152200;
RA Roettgers K., Zufall N., Guiard B., Voos W.;
RT "The ClpB homolog Hsp78 is required for the efficient degradation of
RT proteins in the mitochondrial matrix.";
RL J. Biol. Chem. 277:45829-45837(2002).
RN [11]
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 [12]
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 [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [14]
RP INDUCTION.
RX PubMed=16339719; DOI=10.1128/ec.4.12.2008-2016.2005;
RA Seppae L., Makarow M.;
RT "Regulation and recovery of functions of Saccharomyces cerevisiae chaperone
RT BiP/Kar2p after thermal insult.";
RL Eukaryot. Cell 4:2008-2016(2005).
RN [15]
RP FUNCTION.
RX PubMed=16545993; DOI=10.1016/j.bbamcr.2006.01.007;
RA Lewandowska A., Gierszewska M., Marszalek J., Liberek K.;
RT "Hsp78 chaperone functions in restoration of mitochondrial network
RT following heat stress.";
RL Biochim. Biophys. Acta 1763:141-151(2006).
RN [16]
RP FUNCTION.
RX PubMed=16460754; DOI=10.1016/j.jmb.2006.01.008;
RA von Janowsky B., Major T., Knapp K., Voos W.;
RT "The disaggregation activity of the mitochondrial ClpB homolog Hsp78
RT maintains Hsp70 function during heat stress.";
RL J. Mol. Biol. 357:793-807(2006).
CC -!- FUNCTION: Required, in concert with mitochondrial Hsp70 (SSC1), for the
CC dissociation, resolubilization and refolding of aggregates of damaged
CC proteins in the mitochondrial matrix after heat stress. May extract
CC proteins from aggregates by unfolding and threading them in an ATP-
CC dependent process through the axial channel of the protein hexamer,
CC after which they can be refolded by the Hsp70 chaperone system.
CC Required for resumption of mitochondrial respiratory function, DNA
CC synthesis and morphology after heat stress. Its main role may be
CC maintaining the molecular chaperone SSC1 in a soluble and functional
CC state. Also required for the efficient degradation of proteins by
CC matrix protease PIM1, independent on its protein remodeling activity.
CC {ECO:0000269|PubMed:11231020, ECO:0000269|PubMed:11734006,
CC ECO:0000269|PubMed:12023279, ECO:0000269|PubMed:12237310,
CC ECO:0000269|PubMed:16460754, ECO:0000269|PubMed:16545993,
CC ECO:0000269|PubMed:7500331, ECO:0000269|PubMed:7628444,
CC ECO:0000269|PubMed:8830768}.
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.
CC {ECO:0000269|PubMed:11734006}.
CC -!- INTERACTION:
CC P33416; P10591: SSA1; NbExp=2; IntAct=EBI-8680, EBI-8591;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:8413229, ECO:0000269|PubMed:8830768}.
CC -!- INDUCTION: By heat stress. Expressed at a higher level in respiring
CC cells than in fermenting cells (at protein level).
CC {ECO:0000269|PubMed:16339719, ECO:0000269|PubMed:8413229}.
CC -!- DOMAIN: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per
CC monomer. NBD1 is primarily responsible for ATP hydrolysis. NBD2 is
CC crucial for oligomerization.
CC -!- MISCELLANEOUS: Present with 2990 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; L16533; AAC37362.1; -; Unassigned_DNA.
DR EMBL; Z68329; CAA92715.1; -; Genomic_DNA.
DR EMBL; Z70202; CAA94097.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12098.1; -; Genomic_DNA.
DR PIR; S67315; S67315.
DR RefSeq; NP_010544.3; NM_001180566.3.
DR AlphaFoldDB; P33416; -.
DR SMR; P33416; -.
DR BioGRID; 32308; 122.
DR IntAct; P33416; 2.
DR STRING; 4932.YDR258C; -.
DR iPTMnet; P33416; -.
DR MaxQB; P33416; -.
DR PaxDb; P33416; -.
DR PRIDE; P33416; -.
DR TopDownProteomics; P33416; -.
DR EnsemblFungi; YDR258C_mRNA; YDR258C; YDR258C.
DR GeneID; 851845; -.
DR KEGG; sce:YDR258C; -.
DR SGD; S000002666; HSP78.
DR VEuPathDB; FungiDB:YDR258C; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; P33416; -.
DR OMA; SKMMQGE; -.
DR BioCyc; YEAST:G3O-29829-MON; -.
DR PRO; PR:P33416; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P33416; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0070370; P:cellular heat acclimation; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IMP:SGD.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IGI:SGD.
DR GO; GO:0042026; P:protein refolding; IDA:SGD.
DR GO; GO:0050821; P:protein stabilization; IMP:SGD.
DR GO; GO:0043335; P:protein unfolding; IMP:SGD.
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; 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; 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 PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Coiled coil; Direct protein sequencing;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Repeat;
KW Stress response; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..811
FT /note="Heat shock protein 78, mitochondrial"
FT /id="PRO_0000005500"
FT REGION 98..344
FT /note="NBD1"
FT REGION 467..658
FT /note="NBD2"
FT COILED 345..430
FT /evidence="ECO:0000255"
FT BINDING 143..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 541..548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT MUTAGEN 149
FT /note="K->T: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:11734006"
FT MUTAGEN 547
FT /note="K->T: Impairs oligomerization. Reduces ATPase
FT activity by 92%."
FT /evidence="ECO:0000269|PubMed:11734006"
FT CONFLICT 106
FT /note="T -> K (in Ref. 1; AAC37362)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="R -> A (in Ref. 1; AAC37362)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="D -> V (in Ref. 1; AAC37362)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="E -> K (in Ref. 1; AAC37362)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="A -> P (in Ref. 1; AAC37362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 811 AA; 91336 MW; FC080D1874877075 CRC64;
MLRQATKAPI QKYLQRTQLL RRSTPRIYTI VQCKRSICSF NARPRVANKL LSDIKTNALN
EVAISTCALK SSYGLPNFKR TYVQMRMDPN QQPEKPALEQ FGTNLTKLAR DGKLDPVIGR
DEEIARAIQI LSRRTKNNPC LIGRAGVGKT ALIDGLAQRI VAGEVPDSLK DKDLVALDLG
SLIAGAKYRG EFEERLKKVL EEIDKANGKV IVFIDEVHML LGLGKTDGSM DASNILKPKL
ARGLRCISAT TLDEFKIIEK DPALSRRFQP ILLNEPSVSD TISILRGLKE RYEVHHGVRI
TDTALVSAAV LSNRYITDRF LPDKAIDLVD EACAVLRLQH ESKPDEIQKL DRAIMKIQIE
LESLKKETDP VSVERREALE KDLEMKNDEL NRLTKIWDAE RAEIESIKNA KANLEQARIE
LEKCQREGDY TKASELRYSR IPDLEKKVAL SEKSKDGDKV NLLHDSVTSD DISKVVAKMT
GIPTETVMKG DKDRLLYMEN SLKERVVGQD EAIAAISDAV RLQRAGLTSE KRPIASFMFL
GPTGTGKTEL TKALAEFLFD DESNVIRFDM SEFQEKHTVS RLIGAPPGYV LSESGGQLTE
AVRRKPYAVV LFDEFEKAHP DVSKLLLQVL DEGKLTDSLG HHVDFRNTII VMTSNIGQDI
LLNDTKLGDD GKIDTATKNK VIEAMKRSYP PEFINRIDDI LVFNRLSKKV LRSIVDIRIA
EIQDRLAEKR MKIDLTDEAK DWLTDKGYDQ LYGARPLNRL IHRQILNSMA TFLLKGQIRN
GETVRVVVKD TKLVVLPNHE EGEVVEEEAE K
