HSP104

Summary

Gene Symbol: HSP104
Description: chaperone ATPase HSP104
Alias: chaperone ATPase HSP104
Species: Saccharomyces cerevisiae S288c
Products:     HSP104

Top Publications

  1. Narayanan S, Bösl B, Walter S, Reif B. Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104. Proc Natl Acad Sci U S A. 2003;100:9286-91 pubmed
    ..The molecular chaperone Hsp104 is required to maintain self-replication of [PSI+]...
  2. Bardill J, Dulle J, Fisher J, True H. Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion. Prion. 2009;3:151-60 pubmed
    ..Additionally, we show that the L94A mutation in Rnq1p, which reduces its interaction with Sis1p, prevents Rnq1p from maintaining a prion and inducing [PSI(+)]. ..
  3. Kryndushkin D, Engel A, Edskes H, Wickner R. Molecular chaperone Hsp104 can promote yeast prion generation. Genetics. 2011;188:339-48 pubmed publisher
    ..cerevisiae. We find that overproduction of the disaggregating chaperone, Hsp104, increases the frequency of de novo [URE3] prion formation by the Ure2p of S. cerevisiae and that of C. albicans...
  4. Helsen C, Glover J. A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Prion. 2012;6:234-9 pubmed publisher
    Most prions in yeast form amyloid fibrils that must be severed by the protein disaggregase Hsp104 to be propagated and transmitted efficiently to newly formed buds. Only one yeast prion, [PSI (+) ], is cured by Hsp104 overexpression...
  5. Lee J, Kim J, Biter A, Sielaff B, Lee S, Tsai F. Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor. Proc Natl Acad Sci U S A. 2013;110:8513-8 pubmed publisher
    ..Although Hsp104 is an active ATPase, the recovery of functional protein requires the species-specific cooperation of the Hsp70 ..
  6. Mackay R, Helsen C, Tkach J, Glover J. The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly. Biochemistry. 2008;47:1918-27 pubmed publisher
    The Saccharomyces cerevisiae protein Hsp104, a member of the Hsp100/Clp AAA+ family of ATPases, and its orthologues in plants (Hsp101) and bacteria (ClpB) function to disaggregate and refold thermally denatured proteins following heat ..
  7. Cashikar A, Duennwald M, Lindquist S. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem. 2005;280:23869-75 pubmed
    ..In the yeast Saccharomyces cerevisiae, Hsp104 facilitates disaggregation and reactivates aggregated proteins with assistance from Hsp70 (Ssa1) and Hsp40 (Ydj1)...
  8. Wegrzyn R, Bapat K, Newnam G, Zink A, Chernoff Y. Mechanism of prion loss after Hsp104 inactivation in yeast. Mol Cell Biol. 2001;21:4656-69 pubmed
    ..release factor Sup35 (eRF3), has previously been shown to require intermediate levels of the chaperone protein Hsp104. Here we perform a detailed study on the mechanism of prion loss after Hsp104 inactivation...
  9. Lee S, Sielaff B, Lee J, Tsai F. CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A. 2010;107:8135-40 pubmed publisher
    b>Hsp104 is a ring-forming AAA+ machine that recognizes both aggregated proteins and prion-fibrils as substrates and, together with the Hsp70 system, remodels substrates in an ATP-dependent manner...
  10. Miot M, Reidy M, Doyle S, Hoskins J, Johnston D, Genest O, et al. Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci U S A. 2011;108:6915-20 pubmed publisher
    Yeast Hsp104 and its bacterial homolog, ClpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases...

Detail Information

Publications75

  1. Narayanan S, Bösl B, Walter S, Reif B. Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104. Proc Natl Acad Sci U S A. 2003;100:9286-91 pubmed
    ..The molecular chaperone Hsp104 is required to maintain self-replication of [PSI+]...
  2. Bardill J, Dulle J, Fisher J, True H. Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion. Prion. 2009;3:151-60 pubmed
    ..Additionally, we show that the L94A mutation in Rnq1p, which reduces its interaction with Sis1p, prevents Rnq1p from maintaining a prion and inducing [PSI(+)]. ..
  3. Kryndushkin D, Engel A, Edskes H, Wickner R. Molecular chaperone Hsp104 can promote yeast prion generation. Genetics. 2011;188:339-48 pubmed publisher
    ..cerevisiae. We find that overproduction of the disaggregating chaperone, Hsp104, increases the frequency of de novo [URE3] prion formation by the Ure2p of S. cerevisiae and that of C. albicans...
  4. Helsen C, Glover J. A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Prion. 2012;6:234-9 pubmed publisher
    Most prions in yeast form amyloid fibrils that must be severed by the protein disaggregase Hsp104 to be propagated and transmitted efficiently to newly formed buds. Only one yeast prion, [PSI (+) ], is cured by Hsp104 overexpression...
  5. Lee J, Kim J, Biter A, Sielaff B, Lee S, Tsai F. Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor. Proc Natl Acad Sci U S A. 2013;110:8513-8 pubmed publisher
    ..Although Hsp104 is an active ATPase, the recovery of functional protein requires the species-specific cooperation of the Hsp70 ..
  6. Mackay R, Helsen C, Tkach J, Glover J. The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly. Biochemistry. 2008;47:1918-27 pubmed publisher
    The Saccharomyces cerevisiae protein Hsp104, a member of the Hsp100/Clp AAA+ family of ATPases, and its orthologues in plants (Hsp101) and bacteria (ClpB) function to disaggregate and refold thermally denatured proteins following heat ..
  7. Cashikar A, Duennwald M, Lindquist S. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem. 2005;280:23869-75 pubmed
    ..In the yeast Saccharomyces cerevisiae, Hsp104 facilitates disaggregation and reactivates aggregated proteins with assistance from Hsp70 (Ssa1) and Hsp40 (Ydj1)...
  8. Wegrzyn R, Bapat K, Newnam G, Zink A, Chernoff Y. Mechanism of prion loss after Hsp104 inactivation in yeast. Mol Cell Biol. 2001;21:4656-69 pubmed
    ..release factor Sup35 (eRF3), has previously been shown to require intermediate levels of the chaperone protein Hsp104. Here we perform a detailed study on the mechanism of prion loss after Hsp104 inactivation...
  9. Lee S, Sielaff B, Lee J, Tsai F. CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A. 2010;107:8135-40 pubmed publisher
    b>Hsp104 is a ring-forming AAA+ machine that recognizes both aggregated proteins and prion-fibrils as substrates and, together with the Hsp70 system, remodels substrates in an ATP-dependent manner...
  10. Miot M, Reidy M, Doyle S, Hoskins J, Johnston D, Genest O, et al. Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci U S A. 2011;108:6915-20 pubmed publisher
    Yeast Hsp104 and its bacterial homolog, ClpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases...
  11. Wendler P, Shorter J, Plisson C, Cashikar A, Lindquist S, Saibil H. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell. 2007;131:1366-77 pubmed
    b>Hsp104, a yeast protein-remodeling factor of the AAA+ (ATPases associated with various cellular activities) superfamily, and its homologs in bacteria and plants mediate cell recovery after severe stress by disaggregating denatured ..
  12. Desantis M, Shorter J. Hsp104 drives "protein-only" positive selection of Sup35 prion strains encoding strong [PSI(+)]. Chem Biol. 2012;19:1400-10 pubmed publisher
    ..Here, we demonstrate that Hsp104 remodels the distinct intermolecular contacts of different synthetic Sup35 prion strains in a way that selectively ..
  13. Chartron J, Gonzalez G, Clemons W. A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex. J Biol Chem. 2011;286:34325-34 pubmed publisher
    ..These results allow us to present a structural model of the Sgt2-Get4/Get5-HSC complex. ..
  14. Bagriantsev S, Gracheva E, Richmond J, Liebman S. Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. Mol Biol Cell. 2008;19:2433-43 pubmed publisher
    ..Using a candidate approach, we detected Hsp104, Ssb1/2, Sis1, Sse1, Ydj1, and Sla2 among minor components of the aggregates...
  15. Wendler P, Shorter J, Snead D, Plisson C, Clare D, Lindquist S, et al. Motor mechanism for protein threading through Hsp104. Mol Cell. 2009;34:81-92 pubmed publisher
    The protein-remodeling machine Hsp104 dissolves amorphous aggregates as well as ordered amyloid assemblies such as yeast prions...
  16. Shorter J, Lindquist S. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J. 2008;27:2712-24 pubmed publisher
    Self-templating amyloid forms of Sup35 constitute the yeast prion [PSI(+)]. How the protein-remodelling factor, Hsp104, collaborates with other chaperones to regulate [PSI(+)] inheritance remains poorly delineated...
  17. Wang F, Brown E, Mak G, Zhuang J, Denic V. A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell. 2010;40:159-71 pubmed publisher
    ..Thus, ER-bound TA proteins are sorted at the top of a TMD chaperone cascade that culminates with the formation of Get3-TA protein complexes, which are recruited to the ER membrane for insertion. ..
  18. Schirmer E, Homann O, Kowal A, Lindquist S. Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region. Mol Biol Cell. 2004;15:2061-72 pubmed
    ..That mutations in an 11-amino acid stretch of the MR have such profound and diverse effects suggests the MR plays a central role in regulating Hsp104p function. ..
  19. Shorter J, Lindquist S. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell. 2006;23:425-38 pubmed
    ..A protein-remodeling factor, Hsp104, controls the inheritance of several yeast prions, including those formed by Sup35 and Ure2...
  20. Vacher C, Garcia Oroz L, Rubinsztein D. Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease. Hum Mol Genet. 2005;14:3425-33 pubmed
    ..we have addressed the question in vivo by generating a new transgenic mouse overexpressing the yeast chaperone hsp104, as hsp104 overexpression reduced mutant huntingtin aggregation and toxicity in cell models...
  21. Moosavi B, Wongwigkarn J, Tuite M. Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation. Yeast. 2010;27:167-79 pubmed publisher
    The continued propagation of the yeast [PSI(+)] prion requires the molecular chaperone Hsp104 yet in cells engineered to overexpress Hsp104; prion propagation is impaired leading to the rapid appearance of prion-free [psi(-)] cells...
  22. Glover J, Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 1998;94:73-82 pubmed
    b>Hsp104 is a stress tolerance factor that promotes the reactivation of heat-damaged proteins in yeast by an unknown mechanism. Herein, we demonstrate that Hsp104 functions in this process directly...
  23. 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. 2008;68:87-97 pubmed publisher
    The oligomeric AAA+ chaperone Hsp104 is essential for thermotolerance development and prion propagation in yeast...
  24. Franzmann T, Czekalla A, Walter S. Regulatory circuits of the AAA+ disaggregase Hsp104. J Biol Chem. 2011;286:17992-8001 pubmed publisher
    Yeast Hsp104 is an AAA+ chaperone that rescues proteins from the aggregated state. Six protomers associate to form the functional hexamer. Each protomer contains two AAA+ modules, NBD1 and NBD2...
  25. Helsen C, Glover J. Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104). J Biol Chem. 2012;287:542-56 pubmed publisher
    ..The AAA+ protein disaggregase Hsp104 can sever the amyloid fibrils produced by yeast prions...
  26. Lipi ska N, Zi tkiewicz S, Sobczak A, Jurczyk A, Potocki W, Morawiec E, et al. Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70. J Biol Chem. 2013;288:2857-69 pubmed publisher
    ..Mutations intended to disrupt the putative ionic interactions in yeast Hsp104 and bacterial ClpB disaggregases resulted in remarkable changes of their biochemical properties...
  27. Lum R, Niggemann M, Glover J. Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J Biol Chem. 2008;283:30139-50 pubmed publisher
    The AAA+ molecular chaperone Hsp104 mediates the extraction of proteins from aggregates by unfolding and threading them through its axial channel in an ATP-driven process...
  28. Parsell D, Kowal A, Singer M, Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature. 1994;372:475-8 pubmed
    ..b>Hsp104 protects cells against a variety of stresses, under many physiological conditions, and its function has been ..
  29. Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science. 2004;304:1793-7 pubmed
    The protein-remodeling factor Hsp104 governs inheritance of [PSI+], a yeast prion formed by self-perpetuating amyloid conformers of the translation termination factor Sup35...
  30. Dulle J, Bouttenot R, Underwood L, True H. Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype. J Cell Biol. 2013;203:197-204 pubmed publisher
    ..Furthermore, the nontoxic, self-replicating amyloid conformers of yeast prion proteins have again provided valuable insight into the mechanisms of amyloid formation and propagation in cells. ..
  31. Bösl B, Grimminger V, Walter S. Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J Biol Chem. 2005;280:38170-6 pubmed
    The Hsp104 protein from Saccharomyces cerevisiae is a member of the Hsp100/Clp family of molecular chaperones. It mediates the solubilization of aggregated proteins in an ATP-dependent process assisted by the Hsp70/40 system...
  32. Desantis M, Leung E, Sweeny E, Jackrel M, Cushman Nick M, Neuhaus Follini A, et al. Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell. 2012;151:778-93 pubmed publisher
    It is not understood how Hsp104, a hexameric AAA+ ATPase from yeast, disaggregates diverse structures, including stress-induced aggregates, prions, and ?-synuclein conformers connected to Parkinson disease...
  33. Kohl C, Tessarz P, von der Malsburg K, Zahn R, Bukau B, Mogk A. Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins. Biol Chem. 2011;392:601-8 pubmed publisher
    ..Here, we describe the S. cerevisiae TPR protein Sgt2 as interaction partner of Ssa1 and Hsp104 and as a component of the GET pathway by interacting with Get5...
  34. Sanchez Y, Lindquist S. HSP104 required for induced thermotolerance. Science. 1990;248:1112-5 pubmed
    A heat shock protein gene, HSP104, was isolated from Saccharomyces cerevisiae and a deletion mutation was introduced into yeast cells...
  35. Desantis M, Sweeny E, Snead D, Leung E, Go M, Gupta K, et al. Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. J Biol Chem. 2014;289:848-67 pubmed publisher
    The homologous hexameric AAA(+) proteins, Hsp104 from yeast and ClpB from bacteria, collaborate with Hsp70 to dissolve disordered protein aggregates but employ distinct mechanisms of intersubunit collaboration...
  36. Schirmer E, Ware D, Queitsch C, Kowal A, Lindquist S. Subunit interactions influence the biochemical and biological properties of Hsp104. Proc Natl Acad Sci U S A. 2001;98:914-9 pubmed
    Point mutations in either of the two nucleotide-binding domains (NBD) of Hsp104 (NBD1 and NBD2) eliminate its thermotolerance function in vivo...
  37. 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. 2005;280:23861-8 pubmed
    ..Specifically, we characterized the influence of Hsp104 and Ssa1 on the disassembly of Hsp26 x substrate complexes in vitro and in vivo...
  38. Hattendorf D, Lindquist S. 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. 2002;99:2732-7 pubmed
    b>Hsp104 from Saccharomyces cerevisiae is a hexameric protein with two AAA ATPase domains (N- and C-terminal nucleotide-binding domains NBD1 and NBD2, respectively) per monomer...
  39. Hung G, Masison D. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Genetics. 2006;173:611-20 pubmed
    b>Hsp104 is a hexameric protein chaperone that resolubilizes stress-damaged proteins from aggregates...
  40. Parsell D, Kowal A, Lindquist S. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J Biol Chem. 1994;269:4480-7 pubmed
    ..the mechanism of action of Hsp100 proteins, we have initiated an in vitro analysis of the Saccharomyces cerevisiae Hsp104 protein...
  41. Sielaff B, Tsai F. The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J Mol Biol. 2010;402:30-7 pubmed publisher
    Yeast Hsp104 is a ring-forming ATP-dependent protein disaggregase that, together with the cognate Hsp70 chaperone system, has the remarkable ability to rescue stress-damaged proteins from a previously aggregated state...
  42. Duennwald M, Echeverria A, Shorter J. Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol. 2012;10:e1001346 pubmed publisher
    ..sHsp binding destabilizes Sup35 prions and promotes their disaggregation by Hsp104, Hsp70, and Hsp40...
  43. Nowicki L, Leźnicki P, Morawiec E, Litwińczuk N, Liberek K. Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities. Cell Stress Chaperones. 2012;17:361-73 pubmed publisher
    Besides its beneficial role in thermotolerance, the chaperone protein Hsp104 is involved in the inheritance of yeast Saccharomyces cerevisiae prions...
  44. Wang P, Li J, Weaver C, Lucius A, Sha B. Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions. Acta Crystallogr D Struct Biol. 2017;73:365-372 pubmed publisher
    b>Hsp104 is a yeast member of the Hsp100 family which functions as a molecular chaperone to disaggregate misfolded polypeptides...
  45. Jensen T, Boulay J, Olesen J, Colin J, Weyler M, Libri D. Modulation of transcription affects mRNP quality. Mol Cell. 2004;16:235-44 pubmed
    ..Our results suggest that efficient mRNP assembly is under a kinetic control that is influenced by the rate of transcription. ..
  46. Kushnirov V, Kryndushkin D, Boguta M, Smirnov V, Ter Avanesyan M. Chaperones that cure yeast artificial [PSI+] and their prion-specific effects. Curr Biol. 2000;10:1443-6 pubmed
    ..Although this process is autocatalytic, in vivo it depends on the chaperone Hsp104, whose lack or overexpression can cure [PSI(+)] [2]...
  47. Kirkland P, Reidy M, Masison D. Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity. Genetics. 2011;188:565-77 pubmed publisher
    ..yeast prions [PSI(+)], [URE3], and [PIN(+)] depends on the protein disaggregation machinery that includes Hsp104, Hsp70, and Hsp40 molecular chaperones. Yet, overexpressing Hsp104 cures cells of [PSI(+)] prions...
  48. Mir S, Fiedler D, Cashikar A. Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae. Mol Cell Biol. 2009;29:187-200 pubmed publisher
    In the budding yeast Saccharomyces cerevisiae, the Hsp104-mediated disaggregation of protein aggregates is essential for thermotolerance and to facilitate the maintenance of prions...
  49. Yaguchi S, Tsurugi K. Gts1p activates SNF1-dependent derepression of HSP104 and TPS1 in the stationary phase of yeast growth. J Biol Chem. 2003;278:29760-8 pubmed
    ..Intracellular levels of Hsp104 and trehalose, which were reportedly required for the acquisition of heat tolerance in the stationary phase of ..
  50. Ohta S, Kawai Noma S, Kitamura A, Pack C, Kinjo M, Taguchi H. The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy. Biochem Biophys Res Commun. 2013;442:28-32 pubmed publisher
    ..b>Hsp104, an ATP-dependent disaggregase, and other chaperones are essential to maintain [PSI(+)]...
  51. Sweeny E, Jackrel M, Go M, Sochor M, Razzo B, Desantis M, et al. The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation. Mol Cell. 2015;57:836-49 pubmed publisher
    The structural basis by which Hsp104 dissolves disordered aggregates and prions is unknown...
  52. Erjavec N, Bayot A, Gareil M, Camougrand N, Nystrom T, Friguet B, et al. Deletion of the mitochondrial Pim1/Lon protease in yeast results in accelerated aging and impairment of the proteasome. Free Radic Biol Med. 2013;56:9-16 pubmed publisher
  53. Petitjean M, Teste M, François J, Parrou J. Yeast Tolerance to Various Stresses Relies on the Trehalose-6P Synthase (Tps1) Protein, Not on Trehalose. J Biol Chem. 2015;290:16177-90 pubmed publisher
    ..Altogether, these findings supported the idea that Tps1 is endowed with a regulatory function in energy homeostasis, which is essential to withstand adverse conditions and maintain cellular integrity. ..
  54. Verges K, Smith M, Toyama B, Weissman J. Strain conformation, primary structure and the propagation of the yeast prion [PSI+]. Nat Struct Mol Biol. 2011;18:493-9 pubmed publisher
    ..Thus, effective delivery of infectious particles during cell division is a crucial and conformation-dependent step in prion inheritance. ..
  55. Schirmer E, Lindquist S. Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. Proc Natl Acad Sci U S A. 1997;94:13932-7 pubmed
    ..The inheritance of [PSI+] and the physical state of Sup35 in vivo depend on the protein chaperone Hsp104 (heat shock protein 104)...
  56. Sideri T, Koloteva Levine N, Tuite M, Grant C. Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant. J Biol Chem. 2011;286:38924-31 pubmed publisher
    ..The molecular basis of how yeast and mammalian prions form infectious amyloid-like structures de novo is poorly understood. Our data suggest a causal link between Sup35 protein oxidation and de novo [PSI(+)] prion formation. ..
  57. Klucevsek K, Braun M, Arndt K. The Paf1 complex subunit Rtf1 buffers cells against the toxic effects of [PSI+] and defects in Rkr1-dependent protein quality control in Saccharomyces cerevisiae. Genetics. 2012;191:1107-18 pubmed publisher
    ..identify suppressors of rtf1? rkr1? lethality and found that a mutation in the gene encoding the protein chaperone Hsp104 rescued viability...
  58. Langlois C, Pei F, Sindi S, Serio T. Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo. PLoS Genet. 2016;12:e1006417 pubmed publisher
  59. Kiktev D, Patterson J, Muller S, Bariar B, Pan T, Chernoff Y. Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol. 2012;32:4960-70 pubmed publisher
    ..The yeast prion [PSI(+)] can be eliminated by an excess of the chaperone Hsp104. This effect is reversed by an excess of the chaperone Hsp70-Ssa...
  60. Cherkasov V, Hofmann S, Druffel Augustin S, Mogk A, Tyedmers J, Stoecklin G, et al. Coordination of translational control and protein homeostasis during severe heat stress. Curr Biol. 2013;23:2452-62 pubmed publisher
    ..recovery is intimately linked to disaggregation of damaged proteins present in the mixed assemblies and requires Hsp104 and Hsp70 activity. ..
  61. Torrente M, Castellano L, Shorter J. Suramin inhibits Hsp104 ATPase and disaggregase activity. PLoS ONE. 2014;9:e110115 pubmed publisher
    b>Hsp104 is a hexameric AAA+ protein that utilizes energy from ATP hydrolysis to dissolve disordered protein aggregates as well as amyloid fibers. Interestingly, Hsp104 orthologues are found in all kingdoms of life except animals...
  62. Jackrel M, Shorter J. Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins. Dis Model Mech. 2014;7:1175-84 pubmed publisher
    ..There are no therapies that reverse these protein-misfolding events. We aim to apply Hsp104, a hexameric AAA+ protein from yeast, to target misfolded conformers for reactivation...
  63. Chaudhary R, Kardani J, Singh K, Banerjee R, Roy I. Deciphering the roles of trehalose and Hsp104 in the inhibition of aggregation of mutant huntingtin in a yeast model of Huntington's disease. Neuromolecular Med. 2014;16:280-91 pubmed publisher
  64. Gates S, Yokom A, Lin J, Jackrel M, Rizo A, Kendsersky N, et al. Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104. Science. 2017;357:273-279 pubmed publisher
    ..The Hsp104 disaggregase from Saccharomyces cerevisiae solubilizes stress-induced amorphous aggregates and amyloids...
  65. Powis K, Schrul B, Tienson H, Gostimskaya I, Breker M, High S, et al. Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked. J Cell Sci. 2013;126:473-83 pubmed publisher
    ..Like the generic chaperones Hsp42, Ssa2, Sis1 and Hsp104, we found that Get3 moves reversibly to deposition sites for protein aggregates, hence supporting the ..
  66. Inoue Y, Taguchi H, Kishimoto A, Yoshida M. Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it. J Biol Chem. 2004;279:52319-23 pubmed
    The interaction of Hsp104 with yeast prion fibers made of Sup35NM, a prion-inducing domain of Sup35, was tested...
  67. Rougemaille M, Gudipati R, Olesen J, Thomsen R, Seraphin B, Libri D, et al. Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutants. EMBO J. 2007;26:2317-26 pubmed
    ..Transcription pulse-chase experiments show that HSP104 molecules undergoing quality control in THO/sub2 mutant strains fall into two distinct populations: One that is ..
  68. Chacinska A, Boguta M, Krzewska J, Rospert S. Prion-dependent switching between respiratory competence and deficiency in the yeast nam9-1 mutant. Mol Cell Biol. 2000;20:7220-9 pubmed
    ..Respiratory deficiency of MB43-nam9-1 is overcome by transient overexpression of HSP104, by deletion of HSP104, by transient exposure to guanidine hydrochloride, and by expression of the C-terminal ..
  69. Savistchenko J, Krzewska J, Fay N, Melki R. Molecular chaperones and the assembly of the prion Ure2p in vitro. J Biol Chem. 2008;283:15732-9 pubmed publisher
    ..Finally, the affinities of Ssa1p, Ydj1p, and Hsp104p for Ure2p are determined. Our in vitro observations bring new insight into the mechanism by which molecular chaperones influence the propagation of [URE3]. ..
  70. Lee S, Tsai F. Crystallization and preliminary X-ray crystallographic analysis of a 40 kDa N-terminal fragment of the yeast prion-remodeling factor Hsp104. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007;63:784-6 pubmed
    A 40 kDa N-terminal fragment of Saccharomyces cerevisiae Hsp104 was crystallized in two different crystal forms. Native 1 diffracted to 2.6 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 66.6, b = 75...
  71. Gade V, Kardani J, Roy I. Effect of endogenous Hsp104 chaperone in yeast models of sporadic and familial Parkinson's disease. Int J Biochem Cell Biol. 2014;55:87-92 pubmed publisher
    ..Heterologous expression of the yeast protein remodelling factor Hsp104 has been proposed as a possible therapeutic approach in such disease conditions...
  72. Oberti D, Biasini A, Kirschmann M, Genoud C, Stunnenberg R, Shimada Y, et al. Dicer and Hsp104 function in a negative feedback loop to confer robustness to environmental stress. Cell Rep. 2015;10:47-61 pubmed publisher
    ..variation is buffered by a negative feedback loop that involves the RNase Dicer and the protein disaggregase Hsp104. In the absence of Hsp104, Dicer accumulates in cytoplasmic inclusions and heterochromatin becomes unstable at ..
  73. Borchsenius A, Muller S, Newnam G, Inge Vechtomov S, Chernoff Y. Prion variant maintained only at high levels of the Hsp104 disaggregase. Curr Genet. 2006;49:21-9 pubmed
    ..PSI ( + )] propagation is promoted by moderate levels and antagonized by high levels of the chaperone Hsp104. In agreement with the model postulating that excess Hsp104 acts on [PSI ( + )] by disaggregating prion polymers, ..
  74. Elliott B, Haltiwanger R, Futcher B. Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces cerevisiae. Genetics. 1996;144:923-33 pubmed
    ..The mutant fails to make trehalose and accumulates trehalose-6-phosphate. The other mutation was at the HSP104 locus...