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Mol Cell Biol. 1993 February; 13(2): 869-876

Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70.

Department of Pharmacology, University of Nebraska Medical Center, Omaha 68198-6260.

ABSTRACT

Immunoaffinity purification of hsp90 from chick oviduct cytosol reveals two major proteins, hsp70 and a 60-kDa protein (p60), copurifying with hsp90. A similar result is obtained when hsp90 is immunoaffinity purified from chick liver and brain cytosols, avian fibroblasts, and rabbit reticulocyte lysate. This p60 is the same protein previously identified in certain assembly complexes of chick progesterone receptor generated in a cell-free reconstitution system. Tryptic and cyanogen bromide peptide fragments were generated from gel-purified p60, and partial N-terminal sequences were determined from eight peptides. The sequences show a striking similarity to the sequence of a 63-kDa human protein (IEF SSP 3521) whose abundance is increased in MRC-5 fibroblasts following simian virus 40 transformation. A monoclonal antibody was prepared against avian p60; Western immunoblot analysis showed that p60 was present in each of eight chick tissues examined and in each of the human, rat, rabbit, and Xenopus tissues tested. Immunoaffinity purifications from both chick oviduct cytosol and rabbit reticulocyte lysate using anti-p60 and anti-hsp70 monoclonal antibodies confirm that there is a relatively abundant complex in these extracts containing hsp90, hsp70, and p60. This complex appears to comprise an important functional unit in the assembly of progesterone receptor complexes. However, judging from the abundance and widespread occurrence of this multiprotein complex, hsp90, hsp70, and p60 probably function interactively in other systems as well.

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• Carver, L. A., LaPres, J. J., Jain, S., Dunham, E. E., Bradfield, C. A. (1998). Characterization of the Ah Receptor-associated Protein, ARA9. J. Biol. Chem. 273: 33580-33587 [Abstract] [Full Text]  
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• Couette, B., Jalaguier, S., Hellal-Levy, C., Lupo, B., Fagart, J., Auzou, G., Rafestin-Oblin, M.-E. (1998). Folding Requirements of the Ligand-Binding Domain of the Human Mineralocorticoid Receptor. Mol. Endocrinol. 12: 855-863 [Abstract] [Full Text]  
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• Gale, M. Jr., Blakely, C. M., Hopkins, D. A., Melville, M. W., Wambach, M., Romano, P. R., Katze, M. G. (1998). Regulation of Interferon-Induced Protein Kinase PKR: Modulation of P58IPK Inhibitory Function by a Novel Protein, P52rIPK. Mol. Cell. Biol. 18: 859-871 [Abstract] [Full Text]  
• Prapapanich, V., Chen, S., Smith, D. F. (1998). Mutation of Hip's Carboxy-Terminal Region Inhibits a Transitional Stage of Progesterone Receptor Assembly. Mol. Cell. Biol. 18: 944-952 [Abstract] [Full Text]  
• Dittmar, K. D., Demady, D. R., Stancato, L. F., Krishna, P., Pratt, W. B. (1997). Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone Machinery. THE ROLE OF p23 IS TO STABILIZE RECEPTOR·hsp90 HETEROCOMPLEXES FORMED BY hsp90·p60·hsp70. J. Biol. Chem. 272: 21213-21220 [Abstract] [Full Text]  
• Silverstein, A. M., Galigniana, M. D., Chen, M.-S., Owens-Grillo, J. K., Chinkers, M., Pratt, W. B. (1997). Protein Phosphatase 5 Is a Major Component of Glucocorticoid Receptor·hsp90 Complexes with Properties of an FK506-binding Immunophilin. J. Biol. Chem. 272: 16224-16230 [Abstract] [Full Text]  
• Pratt, W. B., Toft, D. O. (1997). Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones. Endocr. Rev. 18: 306-360 [Abstract] [Full Text]  
• Dittmar, K. D., Pratt, W. B. (1997). Folding of the Glucocorticoid Receptor by the Reconstituted hsp90-based Chaperone Machinery. THE INITIAL hsp90·p60·hsp70-DEPENDENT STEP IS SUFFICIENT FOR CREATING THE STEROID BINDING CONFORMATION. J. Biol. Chem. 272: 13047-13054 [Abstract] [Full Text]  
• Sullivan, W., Stensgard, B., Caucutt, G., Bartha, B., McMahon, N., Alnemri, E. S., Litwack, G., Toft, D. (1997). Nucleotides and Two Functional States of hsp90. J. Biol. Chem. 272: 8007-8012 [Abstract] [Full Text]  
• Irmer, H., Hohfeld, J. (1997). Characterization of Functional Domains of the Eukaryotic Co-chaperone Hip. J. Biol. Chem. 272: 2230-2235 [Abstract] [Full Text]  
• Lassle, M., Blatch, G. L., Kundra, V., Takatori, T., Zetter, B. R. (1997). Stress-inducible, Murine Protein mSTI1. CHARACTERIZATION OF BINDING DOMAINS FOR HEAT SHOCK PROTEINS AND IN VITRO PHOSPHORYLATION BY DIFFERENT KINASES. J. Biol. Chem. 272: 1876-1884 [Abstract] [Full Text]  
• Duina, A. A., Chang, H.-C. J., Marsh, J. A., Lindquist, S., Gaber, R. F. (1996). A Cyclophilin Function in Hsp90-Dependent Signal Transduction. Science 274: 1713-1715 [Abstract] [Full Text]  
• Fang, Y., Fliss, A. E., Robins, D. M., Caplan, A. J. (1996). Hsp90 Regulates Androgen Receptor Hormone Binding Affinity in Vivo. J. Biol. Chem. 271: 28697-28702 [Abstract] [Full Text]  
• Gross, M., Hessefort, S., Olin, A., Reddy, G. (1996). Extensive Sequencing of Tryptic Peptides of a Rabbit Reticulocyte 66-kDa Protein That Promotes Recycling of Hsp 70. HOMOLOGY TO STRESS-RELATED PROTEINS. J. Biol. Chem. 271: 16842-16849 [Abstract] [Full Text]  
• Owens-Grillo, J. K., Czar, M. J., Hutchison, K. A., Hoffmann, K., Perdew, G. H., Pratt, W. B. (1996). A Model of Protein Targeting Mediated by Immunophilins and Other Proteins That Bind to hsp90 via Tetratricopeptide Repeat Domains. J. Biol. Chem. 271: 13468-13475 [Abstract] [Full Text]  
• Dittmar, K. D., Hutchison, K. A., Owens-Grillo, J. K., Pratt, W. B. (1996). Reconstitution of the Steroid Receptor·hsp90 Heterocomplex Assembly System of Rabbit Reticulocyte Lysate. J. Biol. Chem. 271: 12833-12839 [Abstract] [Full Text]  
• Hutchison, K. A., Stancato, L. F., Owens-Grillo, J. K., Johnson, J. L., Krishna, P., Toft, D. O., Pratt, W. B. (1995). The 23-kDa Acidic Protein in Reticulocyte Lysate Is the Weakly Bound Component of the hsp Foldosome That Is Required for Assembly of the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90. J. Biol. Chem. 270: 18841-18847 [Abstract] [Full Text]  
• Robinson, B. L., Morita, T., Toft, D. O., Morris, J. J. (1995). Accelerated recovery of postischemic stunned myocardium after induced expression of myocardial heat-shock protein (HSP70). J. Thorac. Cardiovasc. Surg. 109: 753-764 [Abstract] [Full Text]  
• Tcherepanova, I., Puigserver, P., Norris, J. D., Spiegelman, B. M., McDonnell, D. P. (2000). Modulation of Estrogen Receptor-alpha Transcriptional Activity by the Coactivator PGC-1. J. Biol. Chem. 275: 16302-16308 [Abstract] [Full Text]  
• Johnson, B. D., Chadli, A., Felts, S. J., Bouhouche, I., Catelli, M. G., Toft, D. O. (2000). Hsp90 Chaperone Activity Requires the Full-length Protein and Interaction among Its Multiple Domains. J. Biol. Chem. 275: 32499-32507 [Abstract] [Full Text]  
• Murphy, P. J. M., Kanelakis, K. C., Galigniana, M. D., Morishima, Y., Pratt, W. B. (2001). Stoichiometry, Abundance, and Functional Significance of the hsp90/hsp70-based Multiprotein Chaperone Machinery in Reticulocyte Lysate. J. Biol. Chem. 276: 30092-30098 [Abstract] [Full Text]  
• Scholz, G. M., Cartledge, K., Hall, N. E. (2001). Identification and Characterization of Harc, a Novel Hsp90-associating Relative of Cdc37. J. Biol. Chem. 276: 30971-30979 [Abstract] [Full Text]