Characterization of a lidless form of the molecular chaperone DnaK: Deletion of the lid increases peptide on- and off-rate constants

Journal of Biological Chemistry

Volumn 276, Issue 29, 2001, Pages 27231-27236

  Buczynski, Greg ^b   Slepenkov, Sergey V ^b   Sehorn, Michael G ^b   Witt, Stephan N ^a  

^a LOUISIANA STATE UNIVERSITY HEALTH SCIENCES CENTER   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BIOCHEMISTRY; COMPLEXATION; DISSOCIATION; RATE CONSTANTS; STEREOCHEMISTRY;

CHAPERONE;

POLYPEPTIDES;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; PEPTIDE; PROTEIN DNAK; CHAPERONE; DNAK PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; HEAT SHOCK PROTEIN 70; PRIMER DNA;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; DISSOCIATION; DISSOCIATION CONSTANT; ENZYME ACTIVITY; GENE DELETION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; NUCLEOTIDE SEQUENCE; SPECTROFLUOROMETRY;

ADENOSINE TRIPHOSPHATASES; BASE SEQUENCE; DNA PRIMERS; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; KINETICS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE;

EID: 0035920236     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M100237200     Document Type: Article

References (29)

1. Szabo, A., Langer, T., Schroder, H., Flanagan, J., Bukau, B., and Hartl, F.-U. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 10345-10349
2. Hartl, F. U. (1996) Nature 381, 571-580
3. Bukau, B., and Horwich, A. L. (1998) Cell 92, 351-366
4. Welch, W. J., Eggers, D. K., Hansen, W. J., and Nagata, H. (1998) in Molecular Chaperones in the Life Cycle of Proteins (Fink, A. L., and Goto, U., eds), Marcel Dekker, New York, pp. 71-93
5. Saito, H., and Uchida, H. (1977) J. Mol. Biol. 113, 1-25
6. Yochem, J., Uchida, H., Sunshine, M., Saito, H., Georgopoulos, C. P., and Feiss, M. (1978) Mol. Gen. Genet. 164, 9-14
7. Palleros, D. R., Reid, K. L., Shi, L., Welch, W. J., and Fink, A. L. (1993) Nature 365, 664-666
8. Schmid, D., Baici, A., Gehring, H., and Christen, P. (1994) Science 263, 971-973
9. Buchberger, A., Theyssen, H., Schroder, H., McCarty, J. S., Virgallita, G., Milkereit, P., Reinstein, J., and Bukau, B. (1995) J. Biol. Chem. 270, 16903-16910
10. Theyssen, H., Schuster, H.-P., Packschies, L., Bukau, B., and Reinstein, J. (1996) J. Mol. Biol. 263, 657-670
11. Slepenkov, S. V., and Witt, S. N. (1998) Biochemistry 37, 16749-16756
12. Flaherty, K. M., DeLuca-Flaherty, C., and McKay, D. B. (1990) Nature 346, 623-628
13. Morshauser, R. C., Wang, H., Glynn, G. C., and Zuiderweg, R. P. (1995) Biochemistry 34, 6261-6266
14. Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., and Hendrickson, W. A. (1996) Science 272, 1606-1614
15. Misselwitz, B., Staeck, O., and Rapoport, T. A. (1998) Mol. Cell 2, 593-603
16. Fouchaq, B., Benaroudj, N., Ebel, C., and Ladjimi, M. M. (1999) Eur. J. Biochem. 259, 379-384
17. Pellecchia, M., Montgomery, D. L., Stevens, S. Y., Vander Kooi, C. W., Feng, H.-P., Gierasch, L. M., and Zuiderweg, E. R. P. (2000) Nat. Struct. Biol. 7, 298-303
18. Mayer, M., Schroder, H., Rudiger, S., Paal, K., Laufen, T., and Bukau, B. (2000) Nat. Struct. Biol. 7, 586-593
19. Maru, Y., Afar, D. E., Witte, O., and Shibuya, M. (1996) J. Biol. Chem. 271, 15353-15357
20. Tudyka, T., and Skerra, A. (1997) Prot. Sci. 6, 2180-2187
21. Farr, C. D., Galiano, F. J., and Witt, S. N. (1995) Biochemistry 34, 15574-15582
22. Slepenkov, S. V., and Witt, S. N. (1998) Biochemistry 37, 1015-1024
23. Russell, R., Jordan, R., and McMacken, R. (1998) Biochemistry 37, 596-607
24. Gao, B., Greene, L., and Eisenberg, E. (1994) Biochemistry 33, 2048-2054
25. Gragerov, A., Zeng, L., Zhao, X., Burkholder, W., and Gottesman, M. E. (1994) J. Mol. Biol. 235, 848-854
26. Tack, B. F. P., Dean, J., Eilat, D., Lorenz, P. E., and Schechter, A. N. (1980) J. Biol. Chem. 255, 8842-8847
27. Haugland, R. P. (1992) in Handbook of Fluorescent Probes and Research Chemicals (Larison, K. D., ed.), 5th Ed., Molecular Probes, Eugene, OR
28. Bevington, P. R. (1969) Data Reduction and Error Analysis for the Physical Sciences, McGraw-Hill, New York
29. Hiromi, K. (1979) Kinetics of Fast Enzyme Reactions Theory and Practice, John Wiley & Sons, New York