Interference between proteins Hap46 and Hop/p60, which bind to different domains of the molecular chaperone hsp70/hsc70

Molecular and Cellular Biology

Volumn 18, Issue 11, 1998, Pages 6238-6244

  Gebauer, Mathias ^a   Zeiner, Matthias ^a   Gehring, Ulrich ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 70;

ARTICLE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

HUMULUS; MAMMALIA; TRIXIS;

EID: 0031770820     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.11.6238     Document Type: Article

References (40)

1. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J.-G. Seidman, J. A. Smith, and K. Struhl. 1995. Current protocols in molecular biology. Wiley, New York, N.Y.
2. Bardelli, A., P. Longati, D. Albero, S. Gorupi, C. Schneider, C. Ponzetto, and P. M. Comoglio. 1996. HGF receptor associates with the anti-apoptotic protein Bag-1 and prevents cell death. EMBO J. 15:6205-6212.
3. Boice, J. A., and L. E. Hightower. 1997. A mutational study of the peptide-binding domain of hsc70 guided by secondary structure prediction. J. Biol. Chem. 272:24825-24831.
4. Bukau, B., and A. L. Horwich. 1998. The hsp70 and hsp60 chaperone machines. Cell 92:351-366.
5. Chang, H.-C. J., and S. Lindquist. 1994. Conservation of hsp90 macromolecular complexes in Saccharomyces cerevisiae. J. Biol. Chem. 269:24983-24988.
6. Chappell, T. G., B. B. Konforti, S. L. Schmid, and J. E. Rothman. 1987. The ATPase core of a clathrin uncoating protein. J. Biol. Chem. 262:746-751.
7. Chen, S., V. Prapapanich, R. A. Rimerman, B. Honoré, and D. F. Smith. 1996. Interaction of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70. Mol. Endocrinol. 10:682-693.
8. Cyr, D. M., T. Langer, and M. G. Douglas. 1994. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19:176-181.
9. Demand, J., J. Lüders, and J. Höhfeld. 1998. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol. Cell. Biol. 18:2023-2028.
10. Flaherty, K. M., C. DeLuca-Flaherty, and D. B. McKay. 1990. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346:623-628.
11. Freeman, B. C., M. P. Myers, R. Schumacher, and R. I. Morimoto. 1995. Identification of a regulatory motif in hsp70 that affects ATPase activity, substrate binding and interaction with hdj-1. EMBO J. 14:2281-2292.
12. Fung, K. L., L. Hilgenberg, N. M. Wang, and W. J. Chirico. 1996. Conformations of the nucleotide and polypeptide binding domains of a cytosolic hsp70 molecular chaperone are coupled. J. Biol. Chem. 271:21559-21565.
13. Gebauer, M., M. Zeiner, and U. Gehring. 1997. Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity. FEBS Lett. 417:109-113.
14. Gehring, U. 1998. Steroid hormone receptors and heat shock proteins, p. 167-205. In G. Litwack (ed.), Vitamins and hormones. Advances in research and applications, vol. 54. Academic Press, San Diego, Calif.
15. Gross, M., and S. Hessefort. 1996. Purification and characterization of a 66-kDa protein from rabbit reticulocyte lysate which promotes the recycling of hsp70. J. Biol. Chem. 271:16833-16841.
16. Harrison, C. J., M. Hayer-Hartl, M. Di Liberto, F.-U. Hartl, and J. Kuriyan. 1997. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276:431-435.
17. Hartman, D., and M.-J. Gething. 1996. Normal protein folding machinery, p. 3-24. In U. Feige, R. I. Morimoto, I. Yahara, and B. S. Polla (ed.), Stress-inducible cellular responses. Birkhäuser, Basel, Switzerland.
18. Höhfeld, J., Y. Minami, and F.-U. Hartl. 1995. Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle. Cell 83:589-598.
19. Höhfeld, J., and S. Jentsch. 1997. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16:6209-6216.
20. Hunt, C., and R. I. Morimoto. 1985. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Acad. Sci. USA 82:6455-6459.
21. Johnson, B. D., R. J. Schumacher, E. D. Ross, and D. O. Toft. 1998. Hop modulates hsp70/hsp90 interactions in protein folding. J. Biol. Chem. 273: 3679-3686.
22. Johnson, J. L., and E. A. Craig. 1997. Protein folding in vivo: unraveling complex pathways. Cell 90:201-204.
23. Kullmann, M., J. Schneikert, J. Moll, S. Heck, M. Zeiner, U. Gehring, and A. C. B. Cato. 1998. RAP46 is a negative regulator of glucocorticoid receptor action and hormone induced apoptosis. J. Biol. Chem. 273:14620-14625.
24. Lässie, M., G. L. Blatch, V. Kundra, T. Takatori, and B. R. Zetter. 1997. Stress-inducible, murine protein mSTI1. J. Biol. Chem. 272:1876-1884.
25. Liberek, K., J. Marszalek, D. Ang, C. Georgopoulos, and M. Zylicz. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88:2874-2878.
26. Melki, R., G. Batelier, S. Soulié, and R. C. Williams, Jr. 1997. Cytoplasmic chaperonin containing TCP-1: structural and functional characterization. Biochemistry 36:5817-5826.
27. Morshauser, R. C., H. Wang, G. C. Flynn, and E. R. P. Zuiderweg. 1995. The peptide-binding domain of the chaperone protein hsc70 has an unusual secondary structure topology. Biochemistry 34:6261-6266.
28. Netzer, W. J., and F. U. Hartl. 1998. Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. Trends Biochem. Sci. 23: 68-73.
29. Nicolet, C. M., and E. A. Craig. 1989. Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9:3638-3646.
30. Packham, G., M. Brimmel, and J. L. Cleveland. 1997. Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation. Biochem. J. 328:807-813.
31. Prapapanich, V., S. Chen, S. C. Nair, R. A. Rimerman, and D. F. Smith. 1996. Molecular cloning of human p48, a transient component of progesterone receptor complexes and an hsp70-binding protein. Mol. Endocrinol. 10:420-431.
32. Smith, D. F. 1998. Sequence motifs shared between chaperone components participating in the assembly of progesterone receptor complexes. Biol. Chem. 379:283-288.
33. Sriram, M., J. Osipiuk, B. C. Freeman, R. I. Morimoto, and A. Joachimiak. 1997. Human hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure 5:403-414.
34. Takayama, S., T. Sato, S. Krajewski, K. Kochel, S. Irie, J. A. Millan, and J. C. Reed. 1995. Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity. Cell 80:279-284.
35. Takayama, S., D. N. Bimston, S. Matsuzawa, B. C. Freeman, C. Aime-Sempe, Z. Xie, R. I. Morimoto, and J. C. Reed. 1997. BAG-1 modulates the chaperone activity of hsp70/hsc70. EMBO J. 16:4887-4896.
36. Wang, T.-F., J. Chang, and C. Wang. 1993. Identification of the peptide binding domain of hsc70. J. Biol. Chem. 268:26049-26051.
37. Wilbanks, S. M., L. Chen, H. Tsuruta, K. O. Hodgson, and D. B. McKay. 1995. Solution small-angle X-ray scattering study of the molecular chaperone hsc70 and its subfragments. Biochemistry 34:12095-12106.
38. Zeiner, M., and U. Gehring. 1995. A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning. Proc. Natl. Acad. Sci. USA 92:11465-11469.
39. Zeiner, M., M. Gebauer, and U. Gehring. 1997. Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins. EMBO J. 16:5483-5490.
40. Zhu, X., X. Zhao, W. F. Burkholder, A. Gragerov, C. M. Ogata, M. E. Gottesman, and W. A. Hendrickson. 1996. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272:1606-1614.