Recombinant Saccharomyces cerevisiae Heat shock protein 104 (HSP104), partial

1. Our observations suggest that Hsp104 pore loops have non-overlapping functions in protein disaggregation and together coordinate substrate binding, unfolding, and translocation through the Hsp104 hexamer. PMID: 29175998
2. The role of Hsp104 protein in protein folding in the ribosome and prion propagation PMID: 27633137
3. most yeast prion [PSI(+)] variants arising spontaneously in an hsp104(T160M) strain are cured by restoration of just normal levels of the wild type Hsp104. The curing activity of Hsp104 constitutes an antiprion system, culling many variants of the [PSI+] prion at normal Hsp104 levels. PMID: 28484020
4. this study reports cryo-electron microscopy structures at near-atomic resolution of Hsp104 in different translocation states. PMID: 28619716
5. We demonstrate that physiological levels of ADP highly limit Hsp104 activity. This inhibition, however, is moderated by the Hsp70 chaperone, which allows efficient disaggregation by supporting Hsp104 binding to aggregates but not to non-aggregated, disordered protein substrates. PMID: 27223323
6. Hsp31 can modulate prion status in cooperation with Hsp104 because it inhibits Sup35 aggregate formation and potentiates [PSI(+)] prion curing upon overexpression of Hsp104 PMID: 27690738
7. The cryo-EM structure of wild-type Saccharomyces cerevisiae Hsp104 in the ATP state. PMID: 27478928
8. curing by Hsp104 overexpression depends on both the trimming ability of the fungal Hsp104 homolog and the strength of the [PSI(+)] variant: the greater the trimming activity of the Hsp104 homolog and the weaker the variant, the greater the curing. PMID: 28373280
9. Study found that Tsa1 and Hsp70 physically interact and that hyperoxidation of Tsa1 by hydrogen peroxide is required for the recruitment of the Hsp70 chaperones and the Hsp104 disaggregase to misfolded and aggregated proteins during aging, but not heat stress. PMID: 27264606
10. Kinetics of Formation and Asymmetrical Distribution of Hsp104-Bound Protein Aggregates in Yeast PMID: 27074685
11. ATPase activity at NBD1 or NBD2 is sufficient for Hsp104 potentiation. PMID: 26747608
12. A latent Hsp104 "holdase" activity is sufficient to delay the higher-order assembly of nascent mutant septins PMID: 25673805
13. A key role for Sse1 (Hsp110), in cooperation with Hsp104, in regulating the length and assembly state of [PSI+] prion fibrils in vivo. PMID: 26438827
14. Suramin depends upon ATPase events at both NBDs to exert its maximal effect. Suramin could develop into an important mechanistic probe to study Hsp104 structure and function PMID: 25299406
15. Our results highlight the importance of feedback regulation in building epigenetic memory and uncover Hsp104 and Dicer as homeostatic controllers PMID: 25543137
16. Data indicate that Hsp104-deleted strain resulted in to lower cytotoxicity and increased cell viability. PMID: 25161148
17. Hsp70/40 stimulated the association of Hsp104 with aggregates and increased the duration of this association PMID: 25635051
18. Data show that Hsp104 N-terminal domain is critical for activity of potentiated Hsp104 variants. PMID: 25620563
19. Hsp104 overexpression cures [PSI(+)] by dissolution of the prion seeds in a two-step process. PMID: 24632242
20. Trehalose led to Hsp104 overexpression in mutant human-huntingtin-expressing cells, and resulted in rescue of the endocytotic defect in the yeast cell. PMID: 24248470
21. Regulation of the M-domain of Hsp104 is critical for efficient prion propagation. PMID: 24466354
22. Both mutants Hsp104-G254D and Hsp104-G730D impair weak SUP36 propagation, but are capable of propagating the less stable strong SUP36 variant to some extent. PMID: 24064980
23. this study investigated the interaction between Hsp104 and Sup35 in the lysates of [PSI(+)] cells using fluorescence cross-correlation spectroscopy (FCCS), which can analyze the codiffusion events of different fluorophores. PMID: 24216111
24. we were able to identify the functions of Hsp104 and the osmoprotectant trehalose in solubilising mutant huntingtin. PMID: 24412307
25. Identify soluble, more SDS-sensitive oligomers of Sup35 as prion propagons and show that Hsp104 plays a role in their maintenance. PMID: 24145167
26. full-length Hsp70 on its own could activate the Hsp104 hexamer by promoting intersubunit coordination, suggesting that Hsp70 is an activator of the Hsp104 motor. PMID: 23650362
27. ATPase-deficient Hsp104 mutants did not restore mobility, suggesting that, rather than preventing aggregation, Hsp104 disaggregates mutant SOD1 after it has aggregated PMID: 23583391
28. Hsp104 remodels the distinct intermolecular contacts of different synthetic Sup35 prion strains in a way that selectively amplifies prions encoding strong [PSI(+)] and simultaneously eliminates prions encoding weak [PSI(+)]. PMID: 23177195
29. establish that Hsp104 hexamers adapt different mechanisms of intersubunit collaboration to disaggregate stress-induced aggregates versus amyloid. PMID: 23141537
30. Study investigated the interaction between Hsp104 and Sup35, the priongenic protein in yeast that forms the [PSI ] prion; found that a 20-amino acid segment within the highly-charged, unstructured middle domain of Sup35 contributes to the physical interaction between the middle domain and Hsp104. PMID: 22561166
31. findings point to crucial roles of Hsp70, Sti1, and Hsp90 for efficient curing by overexpressed Hsp104 and provide evidence supporting the earlier suggestion that destruction of prions by protein disaggregation does not adequately explain the curing PMID: 20479121
32. fitted structures confirm that the subunit arrangement of Hsp104 is similar to other AAA+ machines, and place the M-domains on the Hsp104 exterior, where they can potentially interact with large, aggregated proteins. PMID: 20404203
33. Neither Sti1 nor Cpr7 is necessary for prion propagation but the authors show that deletion of the STI1 and CPR7 genes leads to a significant reduction in the generation of [psi(-)] cells by Hsp104 overexpression. PMID: 20014008
34. Hsp104-dependent degradation of mutant ataxin-1 may account for the ability of this chaperone to reduce toxicity caused by polyQ-repeat proteins. PMID: 19995551
35. the direct effects of Hsp104 concentration on the different conformational states of NM, the prion domain of Sup35 were defined PMID: 15155912
36. Hsp104 plus other factor(s) in the yeast cytosol are required for severing Sup35 prion fiber. PMID: 15448141
37. Hsp104 is essential to dissociate substrate proteins from aggregates with incorporated small heat shock proteins PMID: 15843375
38. Hsp104 facilitates disaggregation and reactivates aggregated proteins with assistance from Hsp70 (Ssa1) and Hsp40 (Ydj1) PMID: 15845535
39. upon association with a polypeptide, a conformational change occurs within Hsp104 that strongly reduces the dynamics of nucleotide exchange and commits the bound polypeptide to ATP hydrolysis PMID: 16135516
40. Yeast hsp104 overexpressed in transgenic mice that express the first 171 residues of mutant human huntingtin reduces polyglutamine aggregation and increases survival of Huntington's disease (HD) model mice by 20%. PMID: 16204350
41. Despite retention of [PSI(+)], excess Hsp104 decreases toxicity of overproduced Sup35 in [PSI(+)] strains. PMID: 16307272
42. Hsp104 mutants defective in threading peptides through the hexamer pore had reduced ability to support [PSI(+)] in proportion to protein resolubilization defects PMID: 16582428
43. Hsp104 catalyzes de novo prion nucleation from soluble, native protein. PMID: 16885031
44. HSP104 molecules undergoing quality control in THO/sub2 mutants fall into two populations: One that is quickly degraded after transcription induction and another that escapes rapid decay and accumulates in foci associated with HSP104 transcription site. PMID: 17410208
45. First report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones PMID: 17768355
46. Carbonylated proteins are associated with Hsp104p-containing protein aggregates and these aggregates, like oxidized proteins, are retained in the progenitor cell during cytokinesis by a Sir2p-dependent proces. PMID: 17908928
47. elimination of the whole C-terminal extension results in an Hsp104 molecule which is unable to assemble and becomes aggregation prone at high temperature, highlighting a novel structural role for this region PMID: 18197703
48. Data show that Hsp104 variant that harbour a reduced threading activity were affected in both protein disaggregation and prion propagation, demonstrating that substrate threading represents the common mechanism for processing both substrate classes. PMID: 18312264
49. Hsp104 regulates the gene expression on the posttranscriptional level. PMID: 18389629
50. analysis of chromatin reassembly at HSP104 PMID: 18445041

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KEGG: sce:YLL026W

STRING: 4932.YLL026W