... that the silencing of reporter genes at major native heterochromatic loci (centromeres, telomeres, mating-type locus and rDNA regions) and an artificially induced heterochromatin locus is alleviated in a fission yeast hsp90 mutant, hsp90-G84C . Also, H3K9me2 enrichment at heterochromatin regions, especially...

... the drug did not inhibit GR nuclear export itself. This indicates the existence of a TPR-domain-dependent mechanism for the export of nuclear proteins. The expression balance of those TPR domain proteins bound to the GR–Hsp90 complex may determine the subcellular localization and nucleocytoplasmic...

...)-containing protein that has been proposed to function as an Hsp90 co-chaperone. Morgana deregulation promotes carcinogenesis in both mice and humans while, in Drosophila , loss of mora causes lethality and a complex mitotic phenotype that is rescued by a human morgana transgene. Here, we show that Drosophila...

... localization of the glucocorticoid receptor that is dependent on the time of day is altered at the post-translational level by the absence of REV-ERBα, affecting expression GR target genes. Nuclear receptor Circadian clock Glucocorticoid receptor REV-ERBα HSP90 In mammals, the circadian clock...

... with the heat shock proteins HSP90 and HSP70 via a cytosol-exposed TPR domain. We further show by in vitro and in vivo experiments that AtTPR7 is associated with the Arabidopsis Sec63 homologue, AtERdj2. Interestingly, AtTPR7 can functionally complement a Δ sec71 yeast mutant that is impaired in post...

... that the myosin-binding UCS domain of UNC-45 alone is sufficient to rescue lethal unc-45 null mutants arrested in embryonic muscle development and temperature-sensitive loss-of-function unc-45 mutants defective in worm A-band assembly. Removal of the Hsp90-binding TPR domain of UNC-45 does not affect rescue...

...Gregor P. Lotz; Alexander Brychzy; Stefan Heinz; Wolfgang M. J. Obermann Heat shock protein 90 (HSP90) is considered a specialized molecular chaperone that controls the folding of cell-regulatory proteins such as steroid receptors and kinases. However, its high abundance is suggestive of a more...

... proteins into the endoplasmic reticulum. J. Biol. Chem. 278 , 7034 -7042. Qbadou, S., Becker, T., Mirus, O., Tews, I., Soll, J. and Schleiff, E. ( 2006 ). The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64. EMBO J. 25 , 1836 -1847. Reichert...

... localisation are poorly understood. To understand how cyclin B is targeted to different locations in the cell we have isolated proteins that interact with cyclin B in Drosophila embryo extracts. Here we show that cyclin B interacts with the molecular chaperone Hsp90 and with the MT-associated protein (MAP...

... apoptosis ( Coller et al., 2000 ). In summary, it appears that TRAP-1 plays roles in cell cycle progression, cellular differentiation and apoptosis, but its precise function remains to be elucidated. Although the TRAP-1 protein shows significant homology to the 90 kDa molecular chaperone Hsp90...

...Victoria M. Longshaw; J. Paul Chapple; Maria S. Balda; Michael E. Cheetham; Gregory L. Blatch The co-chaperone murine stress-inducible protein 1 (mSTI1), an Hsp70/Hsp90 organizing protein (Hop) homologue, mediates the assembly of the Hsp70/Hsp90 chaperone heterocomplex. The mSTI1 protein can...

... the proteins interacting with vFLIP in a KSHV-infected primary effusion lymphoma (PEL) cell line, we immunoprecipitated vFLIP and identified four associated proteins by mass spectrometry: IKK components IKKα, β and γ, and the chaperone, Hsp90. Using gel filtration chromatography, we demonstrated that a single...

... function of signal transduction pathways. The relative levels of these proteins may be important, as too little or too much Hsp70 or Hsp90 can result in aberrant growth control, developmental malformations and cell death. Although the functions of heat shock proteins as molecular chaperones have been well...