| Nucleotide exchange is sufficient for Hsp90 functions in vivo. | Nucleotide exchange is sufficient for Hsp90 functions in vivo.
Reidy M, Garzillo K, Masison DC., Free PMC Article | 08/25/2023 |
| Hsp90 and metal-binding J-protein family chaperones are not critically involved in cellular iron-sulfur protein assembly and iron regulation in yeast. | Hsp90 and metal-binding J-protein family chaperones are not critically involved in cellular iron-sulfur protein assembly and iron regulation in yeast.
Carvalho FA, Mühlenhoff U, Braymer JJ, Root V, Stümpfig M, Oliveira CC, Lill R. | 07/13/2023 |
| The Phosphorylation Status of Hsp82 Regulates Mitochondrial Homeostasis During Glucose Sensing in Saccharomyces cerevisiae. | The Phosphorylation Status of Hsp82 Regulates Mitochondrial Homeostasis During Glucose Sensing in Saccharomyces cerevisiae.
Peng G, Hu K, Shang X, Li W, Dou F. | 06/13/2023 |
| The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells. | The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.
Omkar S, Wani TH, Zheng B, Mitchem MM, Truman AW., Free PMC Article | 08/6/2022 |
| Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance. | Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance.
Giannoulis A, Feintuch A, Unger T, Amir S, Goldfarb D., Free PMC Article | 02/26/2022 |
| Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects. | Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.
Hohrman K, Gonçalves D, Morano KA, Johnson JL., Free PMC Article | 09/4/2021 |
| A Single Site Phosphorylation on Hsp82 Ensures Cell Survival during Starvation in Saccharomyces cerevisiae. | A Single Site Phosphorylation on Hsp82 Ensures Cell Survival during Starvation in Saccharomyces cerevisiae.
Shang X, Cao G, Gao H, Li M, Peng G, Ji Y, Zhang Y, Zhang W, Li W, Dou F. | 03/6/2021 |
| Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle. | Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
Biebl MM, Lopez A, Rehn A, Freiburger L, Lawatscheck J, Blank B, Sattler M, Buchner J., Free PMC Article | 02/20/2021 |
| Controlling protein function by fine-tuning conformational flexibility. | Controlling protein function by fine-tuning conformational flexibility.
Schmid S, Hugel T., Free PMC Article | 02/13/2021 |
| Yeast Hsp90 and Hsp70 directly interact through regions homologous to those of E. coli Hsp90Ec and DnaK. Hsp82 and Ssa1 residues directly interact. | Intermolecular Interactions between Hsp90 and Hsp70.
Doyle SM, Hoskins JR, Kravats AN, Heffner AL, Garikapati S, Wickner S., Free PMC Article | 06/20/2020 |
| Data show that the kinetics of closing and opening for the Hsp90 family chaperone HSP82 (HSP82) are slow and that the lower limit for kcat of ATP hydrolysis is approximately 1 s(-1). | The Hsp90 Chaperone: (1)H and (19)F Dynamic Nuclear Magnetic Resonance Spectroscopy Reveals a Perfect Enzyme.
Lee BL, Rashid S, Wajda B, Wolmarans A, LaPointe P, Spyracopoulos L. | 02/29/2020 |
| Chaperoning of eEF2 by Cns1 is essential for yeast viability and requires a defined subset of the Hsp90 machinery as well as the identified eEF2 recruiting factor Hgh1. | The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2.
Schopf FH, Huber EM, Dodt C, Lopez A, Biebl MM, Rutz DA, Mühlhofer M, Richter G, Madl T, Sattler M, Groll M, Buchner J. | 07/20/2019 |
| The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation. | The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation.
Mercier R, Wolmarans A, Schubert J, Neuweiler H, Johnson JL, LaPointe P., Free PMC Article | 04/6/2019 |
| PP2C and PKA may orchestrate glucose sensing and protein folding mediated by HSP90 to enable cells to maintain protein quality for sustained longevity. | Glucose intake hampers PKA-regulated HSP90 chaperone activity.
Chen YC, Jiang PH, Chen HM, Chen CH, Wang YT, Chen YJ, Yu CJ, Teng SC., Free PMC Article | 03/16/2019 |
| Folding and domain interactions of three orthologs of Hsp90 proteins have been reported. | Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy.
Jahn M, Tych K, Girstmair H, Steinmaßl M, Hugel T, Buchner J, Rief M. | 12/1/2018 |
| Hsp90 (Hsp82) and yeast Hsp70 (Ssa1), directly interact in vitro in the absence of the yeast Hop homolog (Sti1), and identify a region in the middle domain of yeast Hsp90 that is required for the interaction. | Functional and physical interaction between yeast Hsp90 and Hsp70.
Kravats AN, Hoskins JR, Reidy M, Johnson JL, Doyle SM, Genest O, Masison DC, Wickner S., Free PMC Article | 11/3/2018 |
| 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. | Hsp90 Is Essential for Chl1-Mediated Chromosome Segregation and Sister Chromatid Cohesion.
Khurana N, Bakshi S, Tabassum W, Bhattacharyya MK, Bhattacharyya S., Free PMC Article | 10/27/2018 |
| 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. | Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle.
Reidy M, Kumar S, Anderson DE, Masison DC., Free PMC Article | 10/13/2018 |
| 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. | Pervasive contingency and entrenchment in a billion years of Hsp90 evolution.
Starr TN, Flynn JM, Mishra P, Bolon DNA, Thornton JW., Free PMC Article | 08/18/2018 |
| 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 | Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway.
Oh JH, Hyun JY, Varshavsky A., Free PMC Article | 05/12/2018 |
| A chemical compound inhibiting the Aha1-Hsp90 chaperone complex | A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.
Stiegler SC, Rübbelke M, Korotkov VS, Weiwad M, John C, Fischer G, Sieber SA, Sattler M, Buchner J., Free PMC Article | 10/21/2017 |
| Report the importance of Hsp90/Sgt1 system in controlling cell plasticity. | The Plasticity of the Hsp90 Co-chaperone System.
Sahasrabudhe P, Rohrberg J, Biebl MM, Rutz DA, Buchner J. | 10/14/2017 |
| 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. | Large Rotation of the N-terminal Domain of Hsp90 Is Important for Interaction with Some but Not All Client Proteins.
Daturpalli S, Knieß RA, Lee CT, Mayer MP. | 07/8/2017 |
| 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. | Importance of cycle timing for the function of the molecular chaperone Hsp90.
Zierer BK, Rübbelke M, Tippel F, Madl T, Schopf FH, Rutz DA, Richter K, Sattler M, Buchner J., Free PMC Article | 05/20/2017 |
| 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. | Molecular Dynamics Simulations Reveal the Mechanisms of Allosteric Activation of Hsp90 by Designed Ligands.
Vettoretti G, Moroni E, Sattin S, Tao J, Agard DA, Bernardi A, Colombo G., Free PMC Article | 02/18/2017 |