Single-step purification and characterization of MBP (maltose binding protein) - DnaJ fusion protein and its utilization for structure-function analysis

Journal of Biochemistry

Volumn 124, Issue 4, 1998, Pages 842-847

  Ishii, Yoshiyuki ^a   Sonezaki, Syuji ^a   Iwasaki, Yasushi ^a   Tauchi, Eiichi ^a   Shingu, Yoshikazu ^a   Okita, Koichi ^a   I Ogawa, Hiroaki ^a   Kato, Yasuhiko ^a   Kondo, Akihiko ^b  

^a KYUSHU INSTITUTE OF TECHNOLOGY   (Japan)

^b KOBE UNIVERSITY   (Japan)

Author keywords

DnaJ; DnaK; Maltose binding protein; Molecular chaperone; Zinc finger like motif

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; EDETIC ACID; HYBRID PROTEIN; IRON; MALTOSE BINDING PROTEIN; PROTEIN DNAK; SULFONIC ACID DERIVATIVE; ZINC FINGER PROTEIN; ZINC ION;

ABSORPTION SPECTROSCOPY; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; EXPRESSION VECTOR; MASS SPECTROMETRY; NONHUMAN; PROTEIN FOLDING; PROTEIN PURIFICATION; STRUCTURE ACTIVITY RELATION; ULTRAVIOLET SPECTROSCOPY;

ESCHERICHIA COLI;

EID: 0031737103     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022188     Document Type: Article

References (38)

1. Sherman, M.Y. and Goldberg, A.L. (1992) Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J. 11, 71-77
2. Skowyra, D., Georgopoulos, C., and Zylicz, M. (1990) The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA-polymerase in an ATP hydrolysis-dependent manner. Cell 62, 939-944
3. Schroder, H., Langer, T., Hartl, F.U., and Bukau, B. (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137-4144
4. Ellis, J. (1987) Proteins as molecular chaperones. Nature 328, 378-379
5. Sunshine, M., Feiss, M., Stuart, J., and Yochem, J. (1977) A new host gene (groPC) necessary for lambda DNA replication. Mol. Gen. Genet. 151, 27-34
6. Saito, H. and Uchida, H. (1977) Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12. J. Mol. Biol. 113, 1-25
7. Saito, H. and Uchida, H. (1978) Organization and expression of the dnaj and dnaK genes of Escherichia coli K12. Mol. Gen. Genet. 164, 1-8
8. Yochem, J., Uchida, H., Sunshine, M., Saito, H., Georgopoulos, C.P., and Feiss, M. (1978) Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication. Mol. Gen. Genet. 164, 9-14
9. Tilly, K. and Yarmolinsky, M. (1989) Participation of Escherichia coli heat shock proteins DnaJ, DnaK and GrpE in P1 plasmid replication. J. Bacteriol. 171, 6025-6029
10. Kawasaki, Y., Wada, C., and Yura, T. (1990) Roles of Escherichia coli heat shock proteins DnaK, DnaJ and GrpE in mini-F plasmid replication. Mol. Gen. Genet. 220, 277-282
11. Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K., and Hartl, F.U. (1992) Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683-689
12. Wild, J., Altman, E., Yura, T., and Gross, C.A. (1992) DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli. Genes Dev. 6, 1165-1172
13. Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C., and Zylic, M. (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88, 2874-2878
14. Szabo, A., Langer, T., Schroder, H., Flanagan, J., Bukau, B., and 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
15. Wawrzynow, A., Banecki, B., Wall, D., Liberek, K., Georgopoulos, C., and Zylicz, M. (1995) ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates. J. Biol. Chem. 270, 19307-19311
16. Wawrzynow, A. and Zylicz, M. (1995) Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J. Biol. Chem. 270, 19300-19306
17. 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for A replication. J. Biol. Chem. 269, 5446-5451
18. Szyperski, T., Pellechia, M., Wall, D., Georgopoulos, C., and Wuthrich, 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
19. Wall, D., Zylicz, M., and Georgopoulos, C. (1995) The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J. Biol. Chem. 270, 2139-2144
20. Caplan, A.J., Cyr, D.M., and Douglas, M.G. (1993) Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins. Mol. Biol. Cell 4, 555-563
21. + gene. A gene that encodes a heat shock protein. J. Biol. Chem. 261, 1782-1785
22. Ohki, M., Tamura, F., Nishimura, S., and Uchida, H. (1986) Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product. J. Biol. Chem. 261, 1778-1781
23. Szabo, A., Korszun, R., Hartl, F.U., and 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
24. Zylicz, M., Yamamoto, T., McKittrick, N., Sell, S., and Georgopoulos, C. (1985) Purification and properties of the dnaJ replication protein of Escherichia coli. J. Biol. Chem. 260, 7591-7598
25. Banecki, B., Liberek, K., Wall, D., Wawrzynow, A., Georgopoulos, C., Bertoli, E., Tanfani, F., and Zylicz, M. (1996) Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone. J. Biol. Chem. 271, 14840-14848
26. Tabor, S. and Richardson, C.C. (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82, 1074-1078
27. Riggs, P. (1992) Expression and purification of maltose binding protein fusion in Short Protocols in Molecular Biology, 2nd ed. (Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K., eds.) pp. 16.21-16.27, Green Publishing Associates, and John Wiley and Sons, New York
28. Garfin, D.E. (1990) One-dimensional gel electrophoresis. Methods Enzymol. 182, 425-441
29. Mizobata, T., Akiyama, Y., Ito, K., Yumoto, N., and Kawata, Y. (1992) Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP. J. Biol. Chem. 267, 17773-17779
30. 2+ release from Escherichia coli aspartate transcarbamoylase. J. Biol. Chem. 259, 14793-14803
31. Fasman, G.D., ed. (1976) Handbook of Biochemistry and Molecular Biology, Protein, Vol. 3, CRC Press, Cleveland
32. Lovenberg, W. and Sobel, B.E. (1965) Rubredoxin; A new electron transfer protein from Clostridium pasteurianum. Proc. Natl. Acad. Sci. USA 54, 193-199
33. Peterson, J.A. and Coon, M.J. (1968) Enzymatic ω-oxidation. J. Biol. Chem. 243, 329-334
34. Lode, E.T. and Coon, M.J. (1971) Enzymatic ω-oxidation. J. Biol. Chem. 246, 791-802
35. Herriott, J.R., Sieker, L.C., Jensen, L.H., and Lovenberg, W. (1970) Structure of rubredoxin: An X-ray study to 2.5 A resolution. J. Mol. Biol. 50, 391-406
36. Watenpaugh, K.D., Sieker, L.C., and Jensen, L.H. (1979) The structure of rubredoxin at 1.2 A resolution. J. Mol. Biol. 131, 509-522
37. Watenpaugh, K.D., Sieker, L.C., and Jensen, L.H. (1980) Crystallographic refinement of rubredoxin at 1.2 A resolution. J. Mol. Biol. 138, 615-633
38. Adman, E.T., Sieker, L.C., Jensen, L.H., Bruschi, M., and LeGall, J. (1977) A structural model of rubredoxin from Desulfovibrio vulgaris at 2 A resolution. J. Mol. Biol. 112, 113-120