Asian-Australasian Journal of Animal Sciences

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

HspBP1 Is the Negative Regulator of the Bovine Progesterone Receptor

  • Park, K.M. (Department of Food & Life Science, Faculty of Life Science and Technology, Sungkyunkwan University Suwon) ;
  • Song, J.W. (Department of Food & Life Science, Faculty of Life Science and Technology, Sungkyunkwan University Suwon)
  • Received : 2002.12.17
  • Accepted : 2003.05.20
  • Published : 2003.09.01
Download PDF
⟨ Previous Next ⟩

Abstract

We have investigated whether HspBP1, a Hsp70 binding protein, could have effect on the assembly of the bovine progesterone receptor (bPR) with a chaperone complex consisting of bovine Hsp90 (bHsp90), bovine Hsp70 (bHsp70), Hop, Ydj-1, and p23. The bPR, isolated in its native conformation, loses its function to interact with progesterone hormone in the absence of this protein complex. However, in the presence of bHsp90, bHsp70, Hop, p23 and Ydj-1, its function could be restored in vitro. Our findings here indicate that the inclusion of HspBP1 to five-protein system prevented the proper assembly of progesterone receptor-chaperone complex and induce the loss of bPR ability to interact with hormone. Immunoprecipitation assays of bPR with HspBP1 show that the presence of HspBP1 did not have any effect on the assembly of Ydj-1 and bHsp70 with the progesterone receptor. However, further assembly of Hsp90, Hop and p23 was completely prevented and the function of the bPR was lost. In vitro competition and protein folding assays indicated that the binding of HspBP1 to bHsp70 prevented the ternary complex formation of bHsp70, bHsp90, and Hop. These results indicate that HspBP1 is a negative regulator of the assembly of Hsp90, Hop and Hsp70, and thus, prevent the proper maturation of unliganded bPR with chaperones assembly system.

Keywords

References

  1. Barent, R. L., S. C. Nair, D. C. Carr, Y. Ruan, R. A. Rimerman, J. Fulton, Y. Zhang and D. F. Smith. 1998. Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes. Mol. Endocrinol. 12:342-354. https://doi.org/10.1210/me.12.3.342
  2. Caplan, A. J., J. Tsai, P. J. Casey and M. G. Douglas. 1992. Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae. J. Biol. Chem. 267:18890-18895.
  3. Chen, S. and D. F. Smith. 1998. Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J. Biol. Chem. 273:35194-35200. https://doi.org/10.1074/jbc.273.52.35194
  4. Cheung, J. and D. F. Smith. 2000. Molecular chaperone interactions with steroid receptors: an update. Mol. Endocrinol. 14:939-946. https://doi.org/10.1210/me.14.7.939
  5. Dittmar, K. D., M. Banach, M. D. Galigniana and W. B. Pratt. 1998. The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex. J. Biol. Chem. 273:7358-7366. https://doi.org/10.1074/jbc.273.13.7358
  6. Hernandez, M. P., A. Chadli and D. O. Toft. 2002. HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor. J. Biol. Chem. 277:11873-11881. https://doi.org/10.1074/jbc.M111445200
  7. Jensen, E. V. 1991. Steroid hormone receptors. In: (Ed. G. Seifert) Cell Receptors. Current Topics in Pathology. Springer-Verlag, Heidelberg, 83:365-431.
  8. Johnson, J. L., T. G. Beito, C. J. Krco and D. O. Toft. 1994. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14:1956-1963. https://doi.org/10.1128/MCB.14.3.1956
  9. Johnson, J. L. and D. O. Toft. 1995. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol. Endocrinol. 10:670-678.
  10. Kabani, M., C. McLellan, D. A. Raynes, V. Guerriero and J. L. Boradsky. 2002. HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. FEBS Lett. 531:339-342. https://doi.org/10.1016/S0014-5793(02)03570-6
  11. Kosano, H., B. Stensgard, M. C. Charlesworth, N. McMahon and D. O. Toft. 1998. The assembly of progesterone receptor-hsp90 complexes using purified proteins. J. Biol. Chem. 273:32973-32979. https://doi.org/10.1074/jbc.273.49.32973
  12. K. H. Liu. 2003. Production of retinol-binding protein by caprine conceptus during th time period of maternal recognition of pregnancy. Asian-Aust. J. Anim. Sci. 16:962-967. https://doi.org/10.5713/ajas.2003.962
  13. Minami, Y., J. Hohfeld, K. Ohtsuka and F. U. Hartl. 1996. Regulation of the heat-shock protein 70 reaction cycle by the mammalian Dna J homolog, Hsp40, J. Biol. Chem. 271:19617-19624. https://doi.org/10.1074/jbc.271.32.19617
  14. Pratt, W. B. and D. O. Toft. 1997. Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones. Endocrine Reviews. 18:306-360. https://doi.org/10.1210/er.18.3.306
  15. Raynes, D. A. and V. Jr. Guerriero. 1998. Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein. J. Biol. Chem. 273:32883-32888. https://doi.org/10.1074/jbc.273.49.32883
  16. Scheufler, C., A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F. U. Hartl and I. Moarefi. 2000. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell. 101:199-210. https://doi.org/10.1016/S0092-8674(00)80830-2
  17. Schumacher, R. J., R. Hurst, W. P. Sullivan, N. J. McMahon, D. O. Toft and R. L. Matts. 1994. ATP-dependent chaparoning activity of reticulocyte lysate. J. Biol. Chem. 269:9493–9499.
  18. Smith, D. F., D. B. Schowalter, S. L. Kost and D. O. Toft. 1990. Reconstitution of progesterone receptor with heat shock proteins. Mol. Endocrinol. 4:1704-1711. https://doi.org/10.1210/mend-4-11-1704
  19. Smith, D. F. and D. O. Toft. 1993. Steroid receptors and their associated proteins. Mol. Endocrinol. 7:4-11. https://doi.org/10.1210/me.7.1.4
  20. Smith, D. F., W. P. Sullivan, T. N. Marion, K. Zaitsu, B. Madden, D. J. McCormick and D. O. Toft. 1993. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol. Cell Biol. 13:869-876.
  21. Smith, D. F., L. Whitesell, S. C. Nair, S. Chen, V. Prapapanich, and R. A. Rimerman. 1995. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell Biol. 15:6804-6812.
  22. Young, J. C. and F. U. Hartl. 2000. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J. 19:5930-5940. https://doi.org/10.1093/emboj/19.21.5930