HSP82 Antibody

1. Folding and domain interactions of three orthologs of Hsp90 proteins have been reported. PMID: 29276035
2. In this study, the authors have established that Chl1, the protein which is involved in maintaining sister chromatid cohesion as well as in preventing chromosome loss, is a direct client of Hsp90. PMID: 29875144
3. Results define two sites on Hsp82: the N-terminal domain (SdN) and C-terminal domain (SdC) which seem to be important for different aspects of the Hsp90 reaction cycle that are regulated by Sti1. SdN function seems to promote a physical interaction of Hsp90 with substrate-bound Hsp70 and SdC-region functions by establishing an Hsp90 conformation crucial for capturing clients and progressing through the reaction cycle. PMID: 29930177
4. Of 98 derived amino acid states that evolved along this lineage, about half compromise fitness when introduced into the reconstructed ancestral Hsp90. And the vast majority of ancestral states reduce fitness when introduced into the extant S. cerevisiae Hsp90. PMID: 29626131
5. results revealed a major role of Nt-acetylation in the Hsp90-mediated protein homeostasis, a strong up-regulation of the Arg/N-end rule pathway in the absence of NatA, and showed that a number of Hsp90 clients are previously unknown substrates of the Arg/N-end rule pathway PMID: 28515311
6. Using crosslinking, hydrogen exchange mass spectrometry, and fluorescence experiments, we demonstrate here that the N-terminal domain of Hsp90 rotates by approximately 180 degrees as compared to the crystal structure of yeast Hsp90 in complex with Sba1 and AMPPNP. PMID: 28363677
7. This study used Hsp90 mutants that modulate ATPase activity and biological function as probes to address the importance of conformational cycling for Hsp90 activity. The study found no correlation between the speed of ATP turnover and the in vivo activity of Hsp90: some mutants with almost normal ATPase activity were lethal, and some mutants with lower or undetectable ATPase activity were viable. PMID: 27723736
8. The impact of different allosteric modulators on the stability, structural and internal dynamics properties of Hsp90 closed state was used to develop a quantitative model relating Hsp90 activation to the presence of a certain compound, using information on the dynamic adaptation of protein conformations to the presence of the ligand, which allows the capture of conformational states relevant in the activation process. PMID: 27032695
9. that, similar to the Hsp70 family, the Hsp90 chaperones also influence yeast prion maintenance, and that immunophilins could regulate protein multimerization independently of their activity as peptidyl-prolyl isomerases PMID: 26473735
10. HSP90 binding regulates Sti1 conformation. PMID: 25851214
11. deletion of a charged linker region in HSP82 causes a pronounced defect Rad51-dependent DNA repair. PMID: 25380755
12. High-resolution NMR solution structures of Tah1 free and in complex with the Hsp90. PMID: 24012479
13. Binding of the glucocorticoid receptor modulates the conformational cycle of Hsp90. PMID: 24613341
14. we systematically investigated the fitness effects of point mutations in a putative substrate binding loop of yeast Hsp90 (Hsp82) over a broad range of expression strengths. PMID: 23825969
15. Suggest that Hsp90 provides an evolutionarily conserved mechanism that links environmental stress to the induction of yeast morphological diversity. PMID: 23434373
16. Charge rich domain in Hsp82p promotes cell growth and maturation of model clients (substrates). PMID: 22660624
17. A specific mutation in yeast Hsp90, hsc82-W296A, resulted in altered transcription patterns genetically linked to the cAMP pathway. PMID: 22461145
18. adaptive value of Hsp90's effects on the relationship between genotype and phenotype PMID: 21205668
19. Hsp90 and the cochaperone Sba1/p23 accumulate in the nucleus of quiescent Saccharomyces cerevisiae cells. PMID: 19889838
20. ATP binding and hydrolysis by Hsp90 are both required for the efficient maturation of glucocorticoid receptor and v-Src. PMID: 19906642
21. effect of Hsp90 mutations on binding and ATPase regulation by the co-chaperones Aha1, Sti1 (Hop), and Sba1 PMID: 15466438
22. An extended network, consisting of 198 putative physical interactions and 451 putative genetic and chemical-genetic interactions, was found to connect Hsp90 to cofactors and substrates involved in a wide range of cellular functions PMID: 15766533
23. potentiates the acquisition of fluconazole resistance; required to maintain resistance acquired by rapid selection but not resistance acquired by gradual selection PMID: 16195452
24. analysis of intrinsic inhibition of the Hsp90 ATPase activity PMID: 16461354
25. Data show that under normal growth conditions, Hsp90 plays a major role in various aspects of the secretory pathway and cellular transport; during environmental stress, Hsp90 is required for the cell cycle, meiosis, and cytokinesis. PMID: 17923092
26. Hsp82p promotes telomerase DNA association and facilitates DNA extension once telomerase is engaged with the DNA PMID: 17954556
27. The conformational transitions are orders of magnitude slower than the ATP-hydrolysis step and thus are the limiting events during the reaction cycle. PMID: 19234467
28. Large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. PMID: 19234469
29. Hsp90 os a part of chaperone system that determins molybdate resistance in Saccharomyces cerevisiae. PMID: 19399909
30. Data show that the Hsp82 chaperone facilitates telomere DNA maintenance by promoting transitions between two operative complexes and by reducing the potential for binding events that would otherwise block the assembly of downstream structures. PMID: 19525972
31. The charged linker region between the N-terminal domain and the middle domain is an important regulator of Hsp90 function. PMID: 19553666

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KEGG: sce:YPL240C

STRING: 4932.YPL240C