Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain

Journal of Molecular Biology

Volumn 260, Issue 2, 1996, Pages 224-235

  Qian, Yan Qiu ^a,c   Patel, Dinshaw ^a   Hartl, F Ulrich ^b   McColl, Damian J ^b  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c GLAXOSMITHKLINE   (United Kingdom)

Author keywords

Heat shock protein (HSP); Molecular chaperones; NMR solution structure; Protein folding; Protein structure

Indexed keywords

HEAT SHOCK PROTEIN;

ARTICLE; HUMAN; NUCLEAR MAGNETIC RESONANCE IMAGING; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SPECTROSCOPY;

EID: 0030581148     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0394     Document Type: Article

References (47)

1. Anil Kumar, Ernst, R. R. & Wüthrich, K. (1980). A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95, 1-6.
2. Bartels, C., Xia, T.-H., Billeter, M., Güntert, P. & Wüthrich, K. (1995). The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR, 6, 1-10.
3. 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. J. Mol. Biol. 155, 321-346.
4. Billeter, M., Kline, A. D., Braun, W., Huber, R. & Wüthrich, K. (1989). Comparison of the high-resolution structures of the α-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals. J. Mol. Biol. 206, 677-687.
5. Buchberger, A., Schroder, H., Buttner, M, Valencia, A. & Bukau, B. (1994). A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nature Struct. Biol. 1, 95-101.
6. Chellaiah, A., Davis, A. & Mohanakumar, T. (1993). Cloning of a unique human homologue of the Escherichia coli DnaJ heat shock protein. Biochim. Biophys. Acta. 1174, 111-113.
7. Cheetham, M. E., Brion, J.-P. & Anderton, B. H. (1992). Human homologues of the bacterial protein DnaJ are preferentially expressed in neurons. Biochem. J. 284, 469-476.
8. Cyr, D. M., Langer, T. & Douglas, M. G. (1994). DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends. Biochem. Sci. 19, 176-181.
9. Feldheim, D., Rothblatt, J. & Schekman, R. (1992). Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol. Cell Biol. 12, 3288-3296.
10. Fesik, S. W. & Zuiderweg, E. R. P. (1988). Heteronuclear three-dimensional NMR spectroscopy. A strategy for simplification of homonuclear two-dimensional NMR spectra. J. Magn. Reson. 78, 588-593.
11. Freeman, B. C., Myers, M. P., Schumacher, R. & Morimoto, R. I. (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. Frydman, J., Nimmesgern, E., Ohtsuka, K. & Hartl, F. U. (1994). Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature, 370, 111-117.
13. Griesinger, C., Sørensen, O. W. & Ernst, R. R. (1985). Two-dimensional correlation of connected NMR transitions. J. Am. Chem. Soc. 107, 6394-6396.
14. 1H spin system identification in macromolecules. J. Amer. Chem. Soc. 110, 7870-7872.
15. Güntert, P. & Wüthrich, K. (1991). Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J. Biomol. NMR, 1, 447-456.
16. Güntert, P. & Wüthrich, K. (1992). FLATT-A new procedure for high-quality baseline correction of multidimensional NMR spectra. J. Magn. Reson. 96, 403-407.
17. 1H NMR assignments and their impact on the precision of protein structure determination in solution. J. Amer. Chem. Soc. 111, 3997-4004.
18. Güntert, P., Braun, W. & Wüthrich, K. (1991a). Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 317, 517-530.
19. Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. & Wüthrich, K. (1991b). Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculations with the programs DIANA, CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217, 531-540.
20. Güntert, P., Berndt, K. D. & Wüthrich, K. (1993). The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination. J. Biomol. NMR, 3, 601-606.
21. 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78). Biochemistry, 34, 5587-5596.
22. Höhfeld, J., Minami, Y. & Hartl, F. U. (1995). Hip, a novel cochaperone involved in the eukaryotic Hsc70/ Hsp40 reaction cycle. Cell, 83, 589-598.
23. Kay, L. E., Keifer, P. & Saarinen, T. (1992). Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665.
24. Kelley, W. L. & Landry, S. J. (1994). Chaperone power in a virus? Trends. Biochem. Sci. 19, 277-278.
25. Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M. K. & Hartl, F. U. (1992) Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature, 356, 683-689.
26. Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C. & Zylicz, M. (1991). Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl Acad. Sci. USA, 88, 2874-2878.
27. Lyman, S. K. & Schekman, R. (1995). Interaction between BiP and Sec63 is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae. J. Cell Biol. 131, 1163-1171.
28. Marion, D., Ikura, M., Tschudin, R. & Bax, A. (1989). Rapid recording of 2D NMR spectra without phase cycling: application to the study of hydrogen exchange in proteins. J. Magn. Reson. 85, 393-399.
29. αβ in the basic pancreatic trypsin inhibitor measured by two-dimensional J-resolved NMR spectroscopy. Eur. J. Biochem. 115, 653-657.
30. Oh, S., Iwahori, A. & Kato, S. (1993). Human cDNA encoding DnaJ protein homologue. Biochim. Biophys. Acta, 1174, 114-116.
31. Ohtsuka, K. (1993). Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ. Biochem. Biophys. Res. Commun. 197, 235-240.
32. Rassow, J., Maarse, A. C., Krainer, E., Kubrich, M., Muller, H., Meijer, M., Craig, E. & Pfanner, N. (1994) Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Biol. 127, 1547-1556.
33. Saiki, R. K., Gelfand, D. H., Stoffel, S., Scharf, S. J., Higuchi, R., Horn, G. T., Mullis, K. B. & Erlich, H. A. (1988). Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science, 239, 487-491.
34. Schlenstedt, G., Harris, S., Risse, B., Lill, R. & Silver, P. (1995). A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J. Cell Biol. 129, 979-988.
35. Szabo, A., Langer, T., Schroder, H., Flanagan, J., Bukau, B. & Hartl, F. U. (1994). The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ and GrpE. Proc. Natl Acad. Sci. USA, 91, 10345-10349.
36. Szabo, A., Korszun, R., Hartl, F. U. & Flanagan, J. (1996). A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J. 15, 408-417.
37. Szyperski, T., Güntert, P., Otting, G. & Wüthrich, K. (1992). Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets. J. Magn. Reson. 99, 552-560.
38. Szyperski, T., Pellecchia, M., Wall, D. Georgopoulos, C. & Wüthrich, K. (1994). NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proc. Natl Acad. Sci. USA, 91, 11343-11347.
39. Ungewickell, E., Ungewickell, H., Holstein, S. E. H., Lindner, R., Prasad, K., Barouch, W., Martin, B., Greene, L. E. & Eisenberg, E. (1995). Role of auxilin in uncoating clathrin-coated vesicles. Nature, 378, 632-635.
40. 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication. J. Biol. Chem. 269, 5446-5451.
41. 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor. J. Mol. Biol. 155, 347-366.
42. Weiner, S. J., Kollman, P. A., Nguyen, D. T. & Case, D. A., (1986). An all atom force field for simulations of proteins and nucleic acids. J. Comp. Chem. 7, 230-252.
43. 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles. J. Mol. Biol. 155, 367-388.
44. 2O solution. J. Magn. Reson. 52, 130-135.
45. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids, Wiley, New York.
46. Xia, T.-H. (1992). Software for determination and visual display of NMR structures of proteins: the distance geometry program DGPLAY and the computer graphics program CONFOR and XAM. Diss. ETH Zurich Nr. 9831.
47. Zinsmaier, K. E., Eberle, K. K., Buchner, E., Walter, N. & Benzer, S. (1994). Paralysis and early death in cysteine string protein mutants of Drosophila. Science, 263, 977-980.