Genomes and Genes
Gene Symbol: HSP104
Description: chaperone ATPase HSP104
Species: Saccharomyces cerevisiae S288c
- Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104Saravanakumar 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+]...
- Dissection and design of yeast prionsLev 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...
- Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prionJ 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(+)]...
- Molecular chaperone Hsp104 can promote yeast prion generationDmitry 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...
- Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteinsJ 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. 1998b>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...
- Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide bindingDouglas 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. 2002b>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...
- Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104Petra Wendler
Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, UK
Cell 131:1366-77. 2007b>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 ..
- Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle regionEric 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...
- Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformersJames Shorter
Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA
Science 304:1793-7. 2004The protein-remodeling factor Hsp104 governs inheritance of [PSI+], a yeast prion formed by self-perpetuating amyloid conformers of the translation termination factor Sup35...
- HSP104 required for induced thermotoleranceY Sanchez
Howard Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637
Science 248:1112-5. 1990A heat shock protein gene, HSP104, was isolated from Saccharomyces cerevisiae and a deletion mutation was introduced into yeast cells...
- Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagationPeter 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. 2008The oligomeric AAA+ chaperone Hsp104 is essential for thermotolerance development and prion propagation in yeast...
- Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfoldingRonnie Lum
Department of Biochemistry, University of Toronto, Ontario M5S 1A8, Canada
J Biol Chem 283:30139-50. 2008The 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...
- Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotidesBenjamin Bösl
Department Chemie, Technische Universitat Munchen, 85747 Garching, Germany
J Biol Chem 280:38170-6. 2005The 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...
- Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's diseaseCoralie 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...
- N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpressionGuo 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. 2006b>Hsp104 is a hexameric protein chaperone that resolubilizes stress-damaged proteins from aggregates...
- Prion-dependent switching between respiratory competence and deficiency in the yeast nam9-1 mutantA 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 ..
- Subunit interactions influence the biochemical and biological properties of Hsp104E 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. 2001Point mutations in either of the two nucleotide-binding domains (NBD) of Hsp104 (NBD1 and NBD2) eliminate its thermotolerance function in vivo...
- Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changesD 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...
- Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104Michael 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. 2010Although propagation of Saccharomyces cerevisiae prions requires Hsp104 protein disaggregating activity, overproducing Hsp104 "cures" cells of [PSI(+)] prions...
- Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicityP 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...
- Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteinsChristian 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...
- Requirements for chromatin reassembly during transcriptional downregulation of a heat shock gene in Saccharomyces cerevisiaeMette 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...
- Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutantTheodora 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...
- Molecular chaperones and the assembly of the prion Ure2p in vitroJimmy 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]...
- [Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level]A A Rubel'
Mol Biol (Mosk) 42:123-30. 2008Yeast 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...
- Regulation of thermotolerance by stress-induced transcription factors in Saccharomyces cerevisiaeNoritaka 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...
- Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein compositionSviatoslav 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...
- Modulation of transcription affects mRNP qualityTorben 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...
- Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prionsJames Shorter
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Stellar Chance Laboratories, Philadelphia, PA 19104, USA
EMBO J 27:2712-24. 2008Self-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...
- CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregationSukyeong 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. 2010b>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...
- Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagationBehrooz Moosavi
Kent Fungal Group, School of Biosciences, University of Kent, Canterbury, UK
Yeast 27:167-79. 2010The 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...
- Hsp104 is essential for the selective degradation in yeast of polyglutamine expanded ataxin-1 but not most misfolded proteins generallyDo 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 ..
- A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulumFei 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...
- Btn3 is a negative regulator of Btn2-mediated endosomal protein trafficking and prion curing in yeastVydehi 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...
- Motor mechanism for protein threading through Hsp104Petra Wendler
Department of Crystallography, Birkbeck College, London, UK
Mol Cell 34:81-92. 2009The protein-remodeling machine Hsp104 dissolves amorphous aggregates as well as ordered amyloid assemblies such as yeast prions...
- Regulatory circuits of the AAA+ disaggregase Hsp104Titus M Franzmann
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA
J Biol Chem 286:17992-8001. 2011Yeast 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...
- A systematic evaluation of the function of the protein-remodeling factor Hsp104 in [PSI+] prion propagation in S. cerevisiae by comprehensive chromosomal mutationsAiko 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 ..
- Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiaeSnober S Mir
Center for Molecular Chaperones, Radiobiology and Cancer Virology, Medical College of Georgia, Augusta, GA 30912, USA
Mol Cell Biol 29:187-200. 2009In the budding yeast Saccharomyces cerevisiae, the Hsp104-mediated disaggregation of protein aggregates is essential for thermotolerance and to facilitate the maintenance of prions...
- The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteinsPeter 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. 2009The yeast AAA(+) chaperone Hsp104 is essential for the development of thermotolerance and for the inheritance of prions...
- The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assemblyRyder G Mackay
Department of Biochemistry, University of Toronto, 1 King s College Circle, Toronto, Ontario, Canada M5S 1A8
Biochemistry 47:1918-27. 2008The 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 ..
- Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104pNika 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 ..
- Mechanism of prion loss after Hsp104 inactivation in yeastR 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...
- Evidence for the interplay between trehalose metabolism and Hsp104 in yeastH Iwahashi
National Institute of Bioscience and Human Technology, Tsukuba, Ibaraki 305 8566, Japan
Appl Environ Microbiol 64:4614-7. 1998Disruption 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)...
- Chaperones that cure yeast artificial [PSI+] and their prion-specific effectsV 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(+)] ...
- 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 stressM 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...
- Mtt1 is a Upf1-like helicase that interacts with the translation termination factors and whose overexpression can modulate termination efficiencyK 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 ..
- Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopyR 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. 1999To 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...
- Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curingG 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]...
- Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrPE 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)...
- Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces cerevisiaeB 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...
- Hsp104 interacts with Hsp90 cochaperones in respiring yeastT 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 ..
- Gts1p activates SNF1-dependent derepression of HSP104 and TPS1 in the stationary phase of yeast growthSo 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 ..
- Crystallization and preliminary X-ray crystallographic analysis of a 40 kDa N-terminal fragment of the yeast prion-remodeling factor Hsp104Sukyeong 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. 2007A 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...
- Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutantsMathieu 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 ..
- A role for the yeast cell cycle/splicing factor Cdc40 in the G1/S transitionYosef 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...
- Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activitiesJames 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...
- Prion variant maintained only at high levels of the Hsp104 disaggregaseAndrey 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, ..
- A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104Anil 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)...
- Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104Martin 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...
- Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever itYuji Inoue
Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatuta, Yokohama 226 8503, Japan
J Biol Chem 279:52319-23. 2004The interaction of Hsp104 with yeast prion fibers made of Sup35NM, a prion-inducing domain of Sup35, was tested...
- Protein disaggregation mediated by heat-shock protein Hsp104D 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 ..
- The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondriaM 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...