Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).

PubWeight™: 1.08‹?› | Rank: Top 10%

🔗 View Article (PMC 3249108)

Published in J Biol Chem on November 11, 2011

Authors

Christopher W Helsen1, John R Glover

Author Affiliations

1: Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Articles citing this

Prions in yeast. Genetics (2012) 2.04

Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics. Chem Biol (2014) 1.71

Sensitivity-Enhanced NMR Reveals Alterations in Protein Structure by Cellular Milieus. Cell (2015) 1.58

Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol (2012) 1.46

Protein rescue from aggregates by powerful molecular chaperone machines. Nat Rev Mol Cell Biol (2013) 1.31

Yeast prions: structure, biology, and prion-handling systems. Microbiol Mol Biol Rev (2015) 0.98

Physiological and environmental control of yeast prions. FEMS Microbiol Rev (2013) 0.97

Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability. PLoS Genet (2013) 0.94

Yeast prions and human prion-like proteins: sequence features and prediction methods. Cell Mol Life Sci (2014) 0.94

The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation. PLoS One (2012) 0.89

Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions. PLoS Genet (2014) 0.87

Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds. Eukaryot Cell (2014) 0.87

Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubes. Protein Sci (2013) 0.86

Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104. J Mol Biol (2015) 0.85

A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Prion (2012) 0.85

Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast. Mol Cell Biol (2014) 0.85

Heterologous aggregates promote de novo prion appearance via more than one mechanism. PLoS Genet (2015) 0.82

Sup35 methionine oxidation is a trigger for de novo [PSI(+)] prion formation. Prion (2015) 0.81

DNA aptamers detecting generic amyloid epitopes. Prion (2012) 0.80

The story of stolen chaperones: how overexpression of Q/N proteins cures yeast prions. Prion (2013) 0.79

Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation. Sci Rep (2016) 0.78

Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variants. Prion (2013) 0.77

Stoichiometry and Affinity of Thioflavin T Binding to Sup35p Amyloid Fibrils. PLoS One (2016) 0.75

Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register. Proc Natl Acad Sci U S A (2017) 0.75

Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo. PLoS Genet (2016) 0.75

Articles cited by this

Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast (1995) 13.20

Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res (1994) 10.72

Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science (1995) 8.66

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell (1998) 7.69

Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science (1996) 7.24

A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature (2000) 6.65

Protein disaggregation mediated by heat-shock protein Hsp104. Nature (1994) 6.27

Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science (2000) 6.16

Conformational variations in an infectious protein determine prion strain differences. Nature (2004) 6.15

Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell (1997) 5.24

Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics (1996) 5.19

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell (2004) 4.90

The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J (1995) 4.68

Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics (1997) 4.21

Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science (2004) 4.01

Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature (2005) 3.86

Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem (2003) 3.53

The structural basis of yeast prion strain variants. Nature (2007) 3.31

The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev (1992) 3.04

Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature (2004) 2.87

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol Cell Biol (1999) 2.69

The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc Natl Acad Sci U S A (1999) 2.44

Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat Genet (2008) 2.43

Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr Microbiol (2001) 2.41

Mechanism of prion loss after Hsp104 inactivation in yeast. Mol Cell Biol (2001) 2.27

Dissection and design of yeast prions. PLoS Biol (2004) 2.19

Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc Natl Acad Sci U S A (2002) 2.15

Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Nature (2008) 2.15

Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell (2006) 2.14

Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem (2004) 2.06

Chaperones that cure yeast artificial [PSI+] and their prion-specific effects. Curr Biol (2000) 1.96

Prion properties of the Sup35 protein of yeast Pichia methanolica. EMBO J (2000) 1.94

Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics (2004) 1.90

The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat Cell Biol (2009) 1.87

Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J (2008) 1.82

Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Mol Cell (2002) 1.82

Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion. EMBO J (2001) 1.70

Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A (2011) 1.70

Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J (2001) 1.69

Red pigment of adenine-deficient yeast Saccharomyces cerevisiae. Biochem Biophys Res Commun (1967) 1.67

Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication. Eukaryot Cell (2005) 1.59

Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell (2007) 1.56

Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'. EMBO J (2001) 1.54

The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J Biol Chem (2003) 1.52

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A (2010) 1.49

Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J (2006) 1.44

The ATPase activity of Hsp104, effects of environmental conditions and mutations. J Biol Chem (1998) 1.41

Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci U S A (2011) 1.37

The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J Mol Biol (2010) 1.36

Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J Biol Chem (2008) 1.34

Prion variant maintained only at high levels of the Hsp104 disaggregase. Curr Genet (2005) 1.33

Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol (2011) 1.27

Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae. Genetics (2001) 1.20

The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants. Genetics (2005) 1.19

Applying Hsp104 to protein-misfolding disorders. Biochem Cell Biol (2010) 1.18

Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochem Cell Biol (2010) 1.18

A size threshold limits prion transmission and establishes phenotypic diversity. Science (2010) 1.18

[Psi(+)] prion generation in yeast: characterization of the 'strain' difference. Yeast (2001) 1.15

Processing of proteins by the molecular chaperone Hsp104. J Mol Biol (2007) 1.14

Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation. J Biol Chem (2004) 1.04

The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae. PLoS One (2009) 1.03

The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans. Eukaryot Cell (2006) 1.03

Biochemical, cell biological, and genetic assays to analyze amyloid and prion aggregation in yeast. Methods Enzymol (2010) 1.02

Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling. Biochemistry (2004) 0.98

Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division. Proc Natl Acad Sci U S A (2005) 0.95

The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion. PLoS One (2009) 0.94

[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain. PLoS One (2011) 0.93

The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly. Biochemistry (2008) 0.92

Prion domain interaction responsible for species discrimination in yeast [PSI+] transmission. Genes Cells (2003) 0.86

Self-perpetuating changes in Sup35 protein conformation as a mechanism of heredity in yeast. Biochem Soc Symp (2001) 0.80

Hsp104 is essential for the selective degradation in yeast of polyglutamine expanded ataxin-1 but not most misfolded proteins generally. Biochem Biophys Res Commun (2009) 0.77

Articles by these authors

BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron (2004) 2.29

Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science (2013) 2.17

Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem (2004) 2.06

Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Mol Cell (2002) 1.82

Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J Biol Chem (2008) 1.34

A multistage system for the automated detection of epileptic seizures in neonatal electroencephalography. J Clin Neurophysiol (2009) 1.20

Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation. J Biol Chem (2004) 1.04

Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling. Biochemistry (2004) 0.98

Detection of pseudosinusoidal epileptic seizure segments in the neonatal EEG by cascading a rule-based algorithm with a neural network. IEEE Trans Biomed Eng (2006) 0.95

Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells. Traffic (2007) 0.93

The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly. Biochemistry (2008) 0.92

The SmpB-tmRNA tagging system plays important roles in Streptomyces coelicolor growth and development. PLoS One (2009) 0.86

A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Prion (2012) 0.85

Enhanced spatio-temporal clustering in the detection of neonatal seizures using context-based rules. Conf Proc IEEE Eng Med Biol Soc (2004) 0.75