HSP104

Summary

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

Top Publications

  1. pmc Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104
    Saravanakumar Narayanan
    Institut für Organische Chemie und Biochemie and Lehrstuhl für Biotechnologie, Technische Universitat Munchen, Lichtenbergstrasse 4, 85747 Garching, Germany
    Proc Natl Acad Sci U S A 100:9286-91. 2003
  2. pmc Dissection and design of yeast prions
    Lev Z Osherovich
    Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, USA
    PLoS Biol 2:E86. 2004
  3. pmc Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion
    J Patrick Bardill
    Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO, USA
    Prion 3:151-60. 2009
  4. pmc Molecular chaperone Hsp104 can promote yeast prion generation
    Dmitry S Kryndushkin
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0830, USA
    Genetics 188:339-48. 2011
  5. pmc Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions
    James Shorter
    Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Stellar Chance Laboratories, Philadelphia, PA 19104, USA
    EMBO J 27:2712-24. 2008
  6. ncbi Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    J R Glover
    Howard Hughes Medical Institute and Department of Molecular Genetics and Cell Biology, The University of Chicago, Illinois 60637, USA
    Cell 94:73-82. 1998
  7. ncbi Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease
    Coralie Vacher
    Department of Medical Genetics, Cambridge Institute for Medical Research, Wellcome MRC Building, Addenbrooke s Hospital, UK
    Hum Mol Genet 14:3425-33. 2005
  8. ncbi Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    James Shorter
    Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA
    Science 304:1793-7. 2004
  9. ncbi Protein disaggregation mediated by heat-shock protein Hsp104
    D A Parsell
    Department of Molecular Genetics and Cell Biology, Howard Hughes Medical Institute, University of Chicago, Illinois 60637
    Nature 372:475-8. 1994
  10. pmc CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
    Sukyeong Lee
    Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA
    Proc Natl Acad Sci U S A 107:8135-40. 2010

Scientific Experts

  • V V Kushnirov
  • Torben Heick Jensen
  • R Kawai
  • H Iwahashi
  • James Shorter
  • Do Hee Lee
  • Sukyeong Lee
  • Peter Tessarz
  • Bernhard Sielaff
  • Michael Reidy
  • Francis T F Tsai
  • Daniel C Masison
  • Petra Wendler
  • Anil G Cashikar
  • Jungsoon Lee
  • Jennifer E Dulle
  • Christopher W Helsen
  • Axel Mogk
  • Bernd Bukau
  • John R Glover
  • Mick F Tuite
  • Susan Lindquist
  • Yongmin Kim
  • Natalia Lipinska
  • Krzysztof Liberek
  • Ewa Morawiec
  • Lukasz Nowicki
  • Martin L Duennwald
  • Rachael Felberbaum
  • Denis A Kiktev
  • Morgan E Desantis
  • Benjamin Bösl
  • Stefan Walter
  • Heather L True
  • Titus M Franzmann
  • Katherine J Verges
  • Dmitry S Kryndushkin
  • P Aaron Kirkland
  • Theodora C Sideri
  • Justin W Chartron
  • Marika Miot
  • Vydehi Kanneganti
  • Christian Kohl
  • Fei Wang
  • Behrooz Moosavi
  • Snober S Mir
  • J Patrick Bardill
  • Susanne Muller
  • Yury O Chernoff
  • A A Rubel'
  • Ryder G Mackay
  • Celia Plisson
  • Noritaka Yamamoto
  • Sviatoslav N Bagriantsev
  • Ronnie Lum
  • Helen R Saibil
  • Mette M Jensen
  • Jimmy Savistchenko
  • E C Schirmer
  • Jonathan S Weissman
  • Aiko Takahashi
  • Nika Erjavec
  • Mathieu Rougemaille
  • Yosef Kaplan
  • Guo Chiuan Hung
  • Andrey S Borchsenius
  • R D Wegrzyn
  • Coralie Vacher
  • Martin Haslbeck
  • G P Newnam
  • Eric C Schirmer
  • Lev Z Osherovich
  • Yuji Inoue
  • Susan L Lindquist
  • Saravanakumar Narayanan
  • So ichi Yaguchi
  • Douglas A Hattendorf
  • Alicja Sobczak
  • S Lindquist
  • Ju Hwang Park
  • Wojciech Potocki
  • Hyangshuk Rhim
  • Magdalena Slusarz
  • Sylwia Rodziewicz-Motowidło
  • Szymon Zietkiewicz
  • Seongman Kang
  • Ja Young Jang
  • Rachel E Bouttenot
  • Krzysztof Gumowski
  • Amadeo B Biter

Detail Information

Publications76

  1. pmc Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104
    Saravanakumar Narayanan
    Institut für Organische Chemie und Biochemie and Lehrstuhl für Biotechnologie, Technische Universitat Munchen, Lichtenbergstrasse 4, 85747 Garching, Germany
    Proc Natl Acad Sci U S A 100:9286-91. 2003
    ..The molecular chaperone Hsp104 is required to maintain self-replication of [PSI+]...
  2. pmc Dissection and design of yeast prions
    Lev Z Osherovich
    Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, USA
    PLoS Biol 2:E86. 2004
    ..Using this knowledge, we have designed novel artificial prions by fusing the replication element of Sup35p to aggregation-prone sequences from other proteins, including pathogenically expanded polyglutamine...
  3. pmc Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion
    J Patrick Bardill
    Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO, USA
    Prion 3:151-60. 2009
    ..Additionally, we show that the L94A mutation in Rnq1p, which reduces its interaction with Sis1p, prevents Rnq1p from maintaining a prion and inducing [PSI(+)]...
  4. pmc Molecular chaperone Hsp104 can promote yeast prion generation
    Dmitry S Kryndushkin
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0830, USA
    Genetics 188:339-48. 2011
    ..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...
  5. pmc Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions
    James Shorter
    Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Stellar Chance Laboratories, Philadelphia, PA 19104, USA
    EMBO J 27:2712-24. 2008
    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...
  6. ncbi Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    J R Glover
    Howard Hughes Medical Institute and Department of Molecular Genetics and Cell Biology, The University of Chicago, Illinois 60637, USA
    Cell 94:73-82. 1998
    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...
  7. ncbi Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease
    Coralie Vacher
    Department of Medical Genetics, Cambridge Institute for Medical Research, Wellcome MRC Building, Addenbrooke s Hospital, UK
    Hum Mol Genet 14:3425-33. 2005
    ..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...
  8. ncbi Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    James Shorter
    Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA
    Science 304:1793-7. 2004
    The protein-remodeling factor Hsp104 governs inheritance of [PSI+], a yeast prion formed by self-perpetuating amyloid conformers of the translation termination factor Sup35...
  9. ncbi Protein disaggregation mediated by heat-shock protein Hsp104
    D A Parsell
    Department of Molecular Genetics and Cell Biology, Howard Hughes Medical Institute, University of Chicago, Illinois 60637
    Nature 372:475-8. 1994
    ..b>Hsp104 protects cells against a variety of stresses, under many physiological conditions, and its function has been ..
  10. pmc CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
    Sukyeong Lee
    Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA
    Proc Natl Acad Sci U S A 107:8135-40. 2010
    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...
  11. pmc A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
    Anil G Cashikar
    Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02143, USA
    J Biol Chem 280:23869-75. 2005
    ..In the yeast Saccharomyces cerevisiae, Hsp104 facilitates disaggregation and reactivates aggregated proteins with assistance from Hsp70 (Ssa1) and Hsp40 (Ydj1)...
  12. pmc N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression
    Guo Chiuan Hung
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0851, USA
    Genetics 173:611-20. 2006
    b>Hsp104 is a hexameric protein chaperone that resolubilizes stress-damaged proteins from aggregates...
  13. ncbi HSP104 required for induced thermotolerance
    Y Sanchez
    Howard Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637
    Science 248:1112-5. 1990
    A heat shock protein gene, HSP104, was isolated from Saccharomyces cerevisiae and a deletion mutation was introduced into yeast cells...
  14. ncbi Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104
    Martin Haslbeck
    Department Chemie, Technische Universitat Munchen, D 85747 Garching, Germany
    J Biol Chem 280:23861-8. 2005
    ..Specifically, we characterized the influence of Hsp104 and Ssa1 on the disassembly of Hsp26 x substrate complexes in vitro and in vivo...
  15. pmc Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region
    Eric C Schirmer
    Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA
    Mol Biol Cell 15:2061-72. 2004
    ..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...
  16. ncbi Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides
    Benjamin Bösl
    Department Chemie, Technische Universitat Munchen, 85747 Garching, Germany
    J Biol Chem 280:38170-6. 2005
    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...
  17. doi Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
    Peter Tessarz
    Universitat Heidelberg, Zentrum fuer Molekulare Biologie Heidelberg ZMBH, DKFZ ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D 69120, Germany
    Mol Microbiol 68:87-97. 2008
    The oligomeric AAA+ chaperone Hsp104 is essential for thermotolerance development and prion propagation in yeast...
  18. pmc Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104
    Petra Wendler
    Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, UK
    Cell 131:1366-77. 2007
    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 ..
  19. pmc Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding
    Douglas A Hattendorf
    Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA
    Proc Natl Acad Sci U S A 99:2732-7. 2002
    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...
  20. pmc Subunit interactions influence the biochemical and biological properties of Hsp104
    E C Schirmer
    Department of Molecular Genetics and Cell Biology and Howard Hughes Medical Institute, University of Chicago, Chicago, IL 60637, USA
    Proc Natl Acad Sci U S A 98:914-9. 2001
    Point mutations in either of the two nucleotide-binding domains (NBD) of Hsp104 (NBD1 and NBD2) eliminate its thermotolerance function in vivo...
  21. pmc Prion-dependent switching between respiratory competence and deficiency in the yeast nam9-1 mutant
    A Chacinska
    Institute of Biochemistry and Biophysics, 02 106 Warsaw, Poland
    Mol Cell Biol 20:7220-9. 2000
    ..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 ..
  22. pmc Mechanism of prion loss after Hsp104 inactivation in yeast
    R D Wegrzyn
    School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, Georgia 30332 0363, USA
    Mol Cell Biol 21:4656-69. 2001
    ..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...
  23. ncbi Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    D A Parsell
    Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637
    J Biol Chem 269:4480-7. 1994
    ..the mechanism of action of Hsp100 proteins, we have initiated an in vitro analysis of the Saccharomyces cerevisiae Hsp104 protein...
  24. pmc Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities
    James Shorter
    Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, Massachusetts 02142, USA
    Mol Cell 23:425-38. 2006
    ..A protein-remodeling factor, Hsp104, controls the inheritance of several yeast prions, including those formed by Sup35 and Ure2...
  25. pmc Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding
    Ronnie Lum
    Department of Biochemistry, University of Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 283:30139-50. 2008
    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...
  26. pmc Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype
    Jennifer E Dulle
    Department of Cell Biology and Physiology, Washington University in St Louis, St Louis, MO 63110
    J Cell Biol 203:197-204. 2013
    ..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. ..
  27. doi Characterization and Hsp104-induced artificial clearance of familial ALS-related SOD1 aggregates
    Yongmin Kim
    Division of Life Sciences, Korea University, Seoul 136 701, South Korea
    Biochem Biophys Res Commun 434:521-6. 2013
    b>Hsp104, a molecular chaperone protein, originates from Saccharomyces cerevisiae and shows potential for development as a therapeutic disaggregase for the treatment of neurodegenerative disorders...
  28. pmc Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor
    Jungsoon Lee
    Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA
    Proc Natl Acad Sci U S A 110:8513-8. 2013
    ..Although Hsp104 is an active ATPase, the recovery of functional protein requires the species-specific cooperation of the Hsp70 ..
  29. pmc Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
    Marika Miot
    Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 108:6915-20. 2011
    Yeast Hsp104 and its bacterial homolog, ClpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases...
  30. pmc Strain conformation, primary structure and the propagation of the yeast prion [PSI+]
    Katherine J Verges
    Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, USA
    Nat Struct Mol Biol 18:493-9. 2011
    ..Thus, effective delivery of infectious particles during cell division is a crucial and conformation-dependent step in prion inheritance...
  31. pmc 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
    Natalia Lipinska
    Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology, University of Gdansk, 80 822 Gdansk, Kladki 24, Poland
    J Biol Chem 288:2857-69. 2013
    ..Mutations intended to disrupt the putative ionic interactions in yeast Hsp104 and bacterial ClpB disaggregases resulted in remarkable changes of their biochemical properties...
  32. pmc Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients
    Morgan E Desantis
    Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    Cell 151:778-93. 2012
    It is not understood how Hsp104, a hexameric AAA+ ATPase from yeast, disaggregates diverse structures, including stress-induced aggregates, prions, and α-synuclein conformers connected to Parkinson disease...
  33. pmc Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities
    Lukasz Nowicki
    Department of Molecular and Cellular Biology, University of Gdansk, Kladki, Gdansk, Poland
    Cell Stress Chaperones 17:361-73. 2012
    Besides its beneficial role in thermotolerance, the chaperone protein Hsp104 is involved in the inheritance of yeast Saccharomyces cerevisiae prions...
  34. pmc A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]
    Christopher W Helsen
    Department of Biochemistry, University of Toronto, Toronto, ON, Canada
    Prion 6:234-9. 2012
    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...
  35. pmc The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner
    Bernhard Sielaff
    Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA
    J Mol Biol 402:30-7. 2010
    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...
  36. pmc A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex
    Justin W Chartron
    Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA
    J Biol Chem 286:34325-34. 2011
    ..These results allow us to present a structural model of the Sgt2-Get4/Get5-HSC complex...
  37. pmc Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans
    Martin L Duennwald
    Boston Biomedical Research Institute, Watertown, Massachusetts, United States of America
    PLoS Biol 10:e1001346. 2012
    ..sHsp binding destabilizes Sup35 prions and promotes their disaggregation by Hsp104, Hsp70, and Hsp40...
  38. pmc Regulation of chaperone effects on a yeast prion by cochaperone Sgt2
    Denis A Kiktev
    School of Biology and Parker H Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, Georgia, USA
    Mol Cell Biol 32:4960-70. 2012
    ..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...
  39. pmc Desumoylation of the endoplasmic reticulum membrane VAP family protein Scs2 by Ulp1 and SUMO regulation of the inositol synthesis pathway
    Rachael Felberbaum
    Departments of Molecular, Cell, and Developmental Biology, Yale University, New Haven, Connecticut, USA
    Mol Cell Biol 32:64-75. 2012
    ..These results provide the first evidence of cross-regulation between the SUMO and inositol pathways, including the sumoylation of an ER membrane protein central to phospholipid synthesis and phosphoinositide signaling...
  40. doi Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation
    Behrooz Moosavi
    Kent Fungal Group, School of Biosciences, University of Kent, Canterbury, UK
    Yeast 27:167-79. 2010
    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...
  41. pmc The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins
    Peter Tessarz
    Universitat Heidelberg, Zentrum fuer Molekulare Biologie Heidelberg, DKFZ ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D 69120, Germany
    Mol Cell Biol 29:3738-45. 2009
    The yeast AAA(+) chaperone Hsp104 is essential for the development of thermotolerance and for the inheritance of prions...
  42. pmc Btn3 is a negative regulator of Btn2-mediated endosomal protein trafficking and prion curing in yeast
    Vydehi Kanneganti
    Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
    Mol Biol Cell 22:1648-63. 2011
    ..Therefore Btn3 is a novel negative regulator of intracellular protein sorting, which may be of importance in the onset of complex I deficiency and Batten disease in humans...
  43. pmc Hsp104 is essential for the selective degradation in yeast of polyglutamine expanded ataxin-1 but not most misfolded proteins generally
    Do Hee Lee
    Department of Biotechnology, Seoul Women s University, Seoul 139 774, Republic of Korea
    Biochem Biophys Res Commun 391:1056-61. 2010
    ..However, another chaperone Hsp104 promoted degradation of mutant ataxin-1 without influencing the solubility or breakdown of short-lived cell ..
  44. pmc Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104
    Michael Reidy
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Mol Cell Biol 30:3542-52. 2010
    Although propagation of Saccharomyces cerevisiae prions requires Hsp104 protein disaggregating activity, overproducing Hsp104 "cures" cells of [PSI(+)] prions...
  45. pmc A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    Fei Wang
    Department of Molecular and Cellular Biology, Harvard University, Northwest Labs, Cambridge, MA 02138, USA
    Mol Cell 40:159-71. 2010
    ..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...
  46. pmc Regulatory circuits of the AAA+ disaggregase Hsp104
    Titus M Franzmann
    Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA
    J Biol Chem 286:17992-8001. 2011
    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...
  47. pmc Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopy
    R Kawai
    National Institute of Bioscience and Human Technology, Agency of Industrial Science and Technology, Tsukuba, Ibaraki, 305 8566, Japan
    Cell Stress Chaperones 4:46-53. 1999
    To reveal the intracellular localization of Hsp104 in the yeast Saccharomyces cerevisiae before and after heat-shock, we performed immunoelectron microscopy after immunogold labeling with anti-Hsp104 antibody...
  48. pmc Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity
    P Aaron Kirkland
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0830, USA
    Genetics 188:565-77. 2011
    ..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...
  49. doi Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins
    Christian Kohl
    Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, DKFZ ZMBH Alliance, Heidelberg, Germany
    Biol Chem 392:601-8. 2011
    ..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...
  50. pmc Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant
    Theodora C Sideri
    Faculty of Life Sciences, University of Manchester, The Michael Smith Building, Oxford Road, Manchester M13 9PT, United Kingdom
    J Biol Chem 286:38924-31. 2011
    ..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...
  51. pmc Motor mechanism for protein threading through Hsp104
    Petra Wendler
    Department of Crystallography, Birkbeck College, London, UK
    Mol Cell 34:81-92. 2009
    The protein-remodeling machine Hsp104 dissolves amorphous aggregates as well as ordered amyloid assemblies such as yeast prions...
  52. pmc A systematic evaluation of the function of the protein-remodeling factor Hsp104 in [PSI+] prion propagation in S. cerevisiae by comprehensive chromosomal mutations
    Aiko Takahashi
    Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo, Tokyo, Japan
    Prion 1:69-77. 2007
    ..Protein-remodeling factor Hsp104 is involved in thermotolerance and [PSI(+)] propagation, however the structure-and-function relationship of Hsp104 ..
  53. ncbi Gts1p activates SNF1-dependent derepression of HSP104 and TPS1 in the stationary phase of yeast growth
    So ichi Yaguchi
    Department of Biochemistry 2, University of Yamanashi, Faculty of Medicine, 1110 Shimokato, Tamaho, Yamanashi 409 3898, Japan
    J Biol Chem 278:29760-8. 2003
    ..Intracellular levels of Hsp104 and trehalose, which were reportedly required for the acquisition of heat tolerance in the stationary phase of ..
  54. pmc Hsp104 interacts with Hsp90 cochaperones in respiring yeast
    T Abbas-Terki
    Departement de Biologie Cellulaire, Universite de Geneve, Sciences III, Geneva, Switzerland
    Mol Cell Biol 21:7569-75. 2001
    ..b>Hsp104, a molecular chaperone required for stress tolerance and for maintenance of [psi(+)] prions in the budding yeast ..
  55. ncbi Chaperones that cure yeast artificial [PSI+] and their prion-specific effects
    V V Kushnirov
    Institute of Experimental Cardiology, Cardiology Research Centre, Third Cherepkovskaya Street 15A, 121552, Moscow, Russia
    Curr Biol 10:1443-6. 2000
    ..Although this process is autocatalytic, in vivo it depends on the chaperone Hsp104, whose lack or overexpression can cure [PSI(+)] [2]...
  56. ncbi Trehalose is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum but not for maintenance of membrane traffic functions after severe heat stress
    M Simola
    Program in Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, Finland
    Mol Microbiol 37:42-53. 2000
    ..protects proteins and membranes under environmental stress conditions, but recently it was shown to assist the Hsp104 chaperone in refolding of heat-damaged proteins in the yeast cytosol...
  57. pmc Mtt1 is a Upf1-like helicase that interacts with the translation termination factors and whose overexpression can modulate termination efficiency
    K Czaplinski
    Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854, USA
    RNA 6:730-43. 2000
    ..Nonsense suppression is apparently not due to induction of [PSI+], even though cooverexpression of HSP104 alleviated the nonsense suppression phenotype observed in cells overexpressing MTT1, suggesting a more direct role ..
  58. pmc Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    G P Newnam
    School of Biology, Georgia Institute of Technology, Atlanta, Georgia 30332 0230, USA
    Mol Cell Biol 19:1325-33. 1999
    ..a prion-like form of the yeast release factor Sup35, requires a specific concentration of the chaperone protein Hsp104: either deletion or overexpression of Hsp104 will cure cells of [PSI]...
  59. pmc Evidence for the interplay between trehalose metabolism and Hsp104 in yeast
    H Iwahashi
    National Institute of Bioscience and Human Technology, Tsukuba, Ibaraki 305 8566, Japan
    Appl Environ Microbiol 64:4614-7. 1998
    Disruption of the HSP104 gene in a mutant which cannot accumulate trehalose during heat shock treatment caused trehalose accumulation (H. Iwahashi, K. Obuchi, S. Fujii, and Y. Komatsu, Lett. Appl. Microbiol 25:43-47, 1997)...
  60. pmc Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP
    E C Schirmer
    Department of Molecular Genetics and Cell Biology and Howard Hughes Medical Institute, University of Chicago, Chicago, IL, 60637, USA
    Proc Natl Acad Sci U S A 94:13932-7. 1997
    ..The inheritance of [PSI+] and the physical state of Sup35 in vivo depend on the protein chaperone Hsp104 (heat shock protein 104)...
  61. pmc Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces cerevisiae
    B Elliott
    Cold Spring Harbor Laboratory, New York 11724, USA
    Genetics 144:923-33. 1996
    ..The mutant fails to make trehalose and accumulates trehalose-6-phosphate. The other mutation was at the HSP104 locus...
  62. ncbi Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it
    Yuji Inoue
    Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatuta, Yokohama 226 8503, Japan
    J Biol Chem 279:52319-23. 2004
    The interaction of Hsp104 with yeast prion fibers made of Sup35NM, a prion-inducing domain of Sup35, was tested...
  63. ncbi Modulation of transcription affects mRNP quality
    Torben Heick Jensen
    Department of Molecular Biology, Aarhus University, C F Møllers Alle, Building 130, 8000 Aarhus C, Denmark
    Mol Cell 16:235-44. 2004
    ..Our results suggest that efficient mRNP assembly is under a kinetic control that is influenced by the rate of transcription...
  64. ncbi A role for the yeast cell cycle/splicing factor Cdc40 in the G1/S transition
    Yosef Kaplan
    Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, 69978, Israel
    Curr Genet 51:123-40. 2007
    ..Finally, we discuss possible mechanisms of suppression by the cDNAs that imply cell cycle regulation by apparently unrelated processes, such as splicing, translation initiation and glycolysis...
  65. pmc Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae
    Snober S Mir
    Center for Molecular Chaperones, Radiobiology and Cancer Virology, Medical College of Georgia, Augusta, GA 30912, USA
    Mol Cell Biol 29:187-200. 2009
    In the budding yeast Saccharomyces cerevisiae, the Hsp104-mediated disaggregation of protein aggregates is essential for thermotolerance and to facilitate the maintenance of prions...
  66. doi Requirements for chromatin reassembly during transcriptional downregulation of a heat shock gene in Saccharomyces cerevisiae
    Mette M Jensen
    Centre for mRNP Biogenesis and Metabolism, Department of Molecular Biology, University of Aarhus, Denmark
    FEBS J 275:2956-64. 2008
    ..In this article, we identify determinants of this reassembly throughout the heat shock protein 104 gene (HSP104) transcription unit...
  67. pmc Molecular chaperones and the assembly of the prion Ure2p in vitro
    Jimmy Savistchenko
    Laboratoire d Enzymologie et Biochimie Structurales, CNRS, 91198 Gif sur Yvette Cedex, France
    J Biol Chem 283:15732-9. 2008
    ..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]...
  68. ncbi [Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level]
    A A Rubel'
    Mol Biol (Mosk) 42:123-30. 2008
    Yeast chaperon Hsp104 is known as a protein which is able to dissociate aggregates of the heat damaged proteins and prion aggregates into smaller pieces or monomers...
  69. pmc Regulation of thermotolerance by stress-induced transcription factors in Saccharomyces cerevisiae
    Noritaka Yamamoto
    Division of Health Sciences, Kanazawa University Graduate School of Medical Science, 5 11 80 Kodatsuno, Kanazawa, Ishikawa 920 0942, Japan
    Eukaryot Cell 7:783-90. 2008
    ..Here, we show that transcriptional activation of their target genes, including HSP104, an antistress chaperone gene, is obligatory for thermotolerance...
  70. pmc Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition
    Sviatoslav N Bagriantsev
    Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607, USA
    Mol Biol Cell 19:2433-43. 2008
    ..Using a candidate approach, we detected Hsp104, Ssb1/2, Sis1, Sse1, Ydj1, and Sla2 among minor components of the aggregates...
  71. ncbi Prion variant maintained only at high levels of the Hsp104 disaggregase
    Andrey S Borchsenius
    School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, 310 Ferst Drive, Atlanta, 30332 0230, USA
    Curr Genet 49:21-9. 2006
    ..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, ..
  72. doi The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly
    Ryder G Mackay
    Department of Biochemistry, University of Toronto, 1 King s College Circle, Toronto, Ontario, Canada M5S 1A8
    Biochemistry 47:1918-27. 2008
    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 ..
  73. pmc Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
    Nika Erjavec
    Department of Cell and Molecular Biology, Goteborg University, 413 90 Goteborg, Sweden
    Genes Dev 21:2410-21. 2007
    ..Deletion of HSP104 resulted in a breakdown of damage asymmetry, and overproduction of Hsp104p partially restored damage retention in ..
  74. pmc Crystallization and preliminary X-ray crystallographic analysis of a 40 kDa N-terminal fragment of the yeast prion-remodeling factor Hsp104
    Sukyeong Lee
    Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA
    Acta Crystallogr Sect F Struct Biol Cryst Commun 63:784-6. 2007
    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...
  75. pmc Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutants
    Mathieu Rougemaille
    Centre National de la Recherche Scientifique, Centre de Genetique Moleculaire, Gif sur Yvette, France
    EMBO J 26:2317-26. 2007
    ..Transcription pulse-chase experiments show that HSP104 molecules undergoing quality control in THO/sub2 mutant strains fall into two distinct populations: One that is ..
  76. pmc The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria
    M Schmitt
    Institut für Physiologische Chemie der Universität München, Federal Republic of Germany
    J Cell Biol 134:1375-86. 1996
    ..When expressed in the cytosol, Hsp78 can substitute for the homologous heat shock protein Hsp104 in mediating cellular thermotolerance, suggesting a conserved mode of action of the two proteins...