The Agrobacterium tumefaciens DnaK: ATPase cycle, oligomeric state and chaperone properties

International Journal of Biochemistry and Cell Biology

Volumn 40, Issue 4, 2008, Pages 804-812

  Boshoff, Aileen ^a   Stephens, Linda L ^a   Blatch, Gregory L ^a  

^a RHODES UNIVERSITY   (South Africa)

Author keywords

Agrobacterium tumefaciens; ATPase; DnaK; Escherichia coli; Oligomerisation; Thermal aggregation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; MALATE DEHYDROGENASE; OLIGOMER; PROTEIN DNAK;

AMINO TERMINAL SEQUENCE; ARTICLE; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBICITY; MOLECULAR WEIGHT; NONHUMAN; PROTEIN DOMAIN; RHIZOBIUM; THERMAL ANALYSIS;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; CHROMATOGRAPHY, GEL; DIMERIZATION; GENETIC COMPLEMENTATION TEST; HYDROLYSIS; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN STRUCTURE, TERTIARY; RHIZOBIUM RADIOBACTER;

AGROBACTERIUM TUMEFACIENS; ESCHERICHIA COLI;

EID: 39649089380     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2007.10.017     Document Type: Article

References (34)

1. Basha E., Lee G.J., Demeler B., and Vierling E. Chaperone activity of cytosolic small heat shock proteins from wheat. European Journal of Biochemistry 271 (2004) 1426-1436
2. Benaroudj N., Batelier G., Triniolles F., and Ladjimi M.M. Self association of the molecular chaperone Hsc70. Biochemistry 34 (1995) 15282-15290
3. Benaroudj N., Fouchaq B., and Ladjimi M.M. The COOH-terminal peptide binding domain is essential for self-association of the molecular chaperone Hsc70. The Journal of Biological Chemistry 272 (1997) 8744-8851
4. Benaroudj N., Triniolles F., and Ladjimi M.M. Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone Hsc70. The Journal of Biological Chemistry 271 (1996) 18471-18476
5. Boshoff A., Hennessy F., and Blatch G.L. The in vivo and in vitro characterization of DnaK from Agrobacterium tumefaciens RUOR. Protein Expression and Purification 38 (2004) 161-169
6. Brodsky J.L., and McCracken A.A. ER protein quality control and proteasome-mediated protein degradation. Seminars in Cellular and Developmental Biology 10 (1999) 507-513
7. Burkholder W.F., Panagiotidis C.A., Silverstein S.J., Cegielska A., Gottesman M.E., and Gaitanaris G.A. Isolation and characterization of an Escherichia coli DnaK mutant with impaired ATPase activity. Journal of Molecular Biology 242 (1994) 364-377
8. Chou C.-C., Forouhar F., Yeh Y.-H., Shr H.-L., Wang C., and Hsiao C.-D. Crystal structure of the C-terminal 10 kDa subdomain of Hsc70. The Journal of Biological Chemistry 278 (2003) 30311-30316
9. Eggers D.K., Welch W.J., and Hansen W.J. Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Molecular Biology of the Cell 8 (1997) 1559-1573
10. Fouchaq B., Beraroudj N., Ebel C., and Ladjimi M.M. Oligiomerization of the 17-kDa peptide-binding domain of the molecular chaperone Hsc70. European Journal of Biochemistry 259 (1999) 379-384
11. Goloubinoff P., Mogk A., Zvi A.P.B., Tomoyasu T., and Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proceedings of the National Academy of Sciences 96 (1999) 13732-13737
12. Hamman B.D., Hendershot L.M., and Johnson A.E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92 (1998) 747-758
13. Hartman D.J., Surin B.P., Dixon N.E., Hoogenraad N.J., and Hoj P.B. Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro. Proceedings of the National Academy of Sciences 90 (1993) 2276-2280
14. Hennessy F., Boshoff A., and Blatch G.L. Rational mutagenesis of the J domain identifies residues critical to the in vivo function of the Agrobacterium tumefaciens DnaJ. International Journal of Biochemistry and Cell Biology 37 (2005) 177-191
15. Liberek K., Marszalek J., Ang D., Georgopoulos C., and Zylicz M. Escherichia coli DnaJ and GrpE heat proteins jointly stimulate ATPase activity of DnaK. Proceedings of the National Academy of Sciences 88 (1991) 2874-2878
16. Mayer M.P., and Bukau B. Hsp70 chaperones: Cellular functions and molecular mechanisms. Cellular and Molecular Life Sciences 62 (2005) 670-684
17. Mayer M.P., Schröder H., Rüdiger S., Paal K., Laufen T., and Bukau B. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nature: Structure and Molecular Biology 7 (2000) 586-593
18. McCarty J.S., Buchberger A., Reinstein J., and Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. Journal of Molecular Biology 249 (1995) 126-137
19. Nemoto T.K., Fukuma Y., Itoh H., Takashi T., and Ono T. A disulphide bridge mediated by cysteine 574 is formed in the dimer of 70 kDa heat shock protein. Journal of Biochemistry 139 (2006) 677-687
20. Ohno M., Kitabatake N., and Tani F. Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity. FEBS Letters 576 (2004) 381-386
21. Packschies L., Theyssen H., Buchberger A., Bukau B., Goody R.S., and Reinstein J. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry 36 (1997) 3417-3422
22. Palleros D.R., Reid K., Shi L., and Fink A.L. DnaK ATPase activity revisited. FEBS Letters 336 (1993) 124-128
23. Rüdiger S., Mayer M.P., Schneider-Mergener J., and Bukau B. Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. Journal of Molecular Biology 304 (2000) 245-251
24. Russell R., Jordan R., and McMacken R. Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone. Biochemistry 37 (1998) 596-607
25. Schönfeld H.-J., Schmidt D., Schröder H., and Bukau B. The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of the DnaK and GrpE components. The Journal of Biological Chemistry 270 (1995) 2183-2189
26. Silberg J.J., and Vickery L.E. Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli. The Journal of Biological Chemistry 275 (2000) 7779-7786
27. Skowyra D., Georgopoulos C., and Zylicz M. The Escherichia coli dnaK gene product, the Hsp70 homologue, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. Cell 62 (1990) 939-944
28. Slepenkov S.V., and Witt S.N. The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase?. Molecular Microbiology 45 (2002) 1197-1206
29. Spence J., Cegielska A., and Georgopoulos C. Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation. Journal of Bacteriology 172 (1990) 7157-7166
30. Theyssen H., Schuster H.P., Packschies L., Bukau B., and Reinstein J. The second step of ATP binding to DnaK induces peptide release. Journal of Molecular Biology 263 (1996) 657-670
31. Worrall L.J., and Walkinshaw M.D. Crystal structure of the C-terminal three-helix bundle subdomain of C. elegans Hsp70. Biochemical and Biophysical Research Communications 357 (2007) 105-110
32. Zhu X., Zhao X., Burkholder W., Gragerov A., Ogata C.M., Gottesman M.E., et al. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272 (1996) 1606-1614
33. Zylicz M., Ang D., Liberek K., and Georgopoulos C. Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: The role of the DnaK, DnaJ and GrpE heat shock proteins. EMBO Journal 8 (1989) 1601-1608
34. Zylicz M., and Georgopoulos C. Purification and properties of the Escherichia coli dnaK replication protein. The Journal of Biological Chemistry 259 (1984) 8820-8825