Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

EMBO Journal

Volumn 16, Issue 7, 1997, Pages 1501-1507

  Rüdiger, Stefan ^c   Germeroth, Lothar ^a   Schneider Mergener, Jens ^b   Bukau, Bernd ^c  

^a Jerini Bio Tools GmbH   (Germany)

^b CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^c UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

Cellulose bound peptide libraries; Heat shock proteins; Hsp70; Protein folding; Spot synthesis

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELLULOSE; CHAPERONE; HEAT SHOCK PROTEIN 70; PEPTIDE; PROTEIN DNAK;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; ENZYME SPECIFICITY; ESCHERICHIA COLI; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; STATISTICS;

ALGORITHMS; AMINO ACID SEQUENCE; BINDING SITES; CELLULOSE; COMPUTER SIMULATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; INFORMATION SYSTEMS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; REPRODUCIBILITY OF RESULTS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 0030976048     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.7.1501     Document Type: Article

References (32)

1. Blond-Elguindi,S., Cwirla,S.E., Dower,W.J., Lipshutz,R.J., Sprang,S.R., Sambrook,J.F. and Gething,M.-J.H. (1993) Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell, 75, 717-728.
2. Buchberger,A., Valencia,A., McMacken,R., Sander,C. and Bukau,B. (1994) The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J., 13, 1687-1695.
3. Burkholder,W.E. Zhao,X., Zhu,X. and Hendrickson,W.A. (1996) Mutations in the C-terminal fragment of DnaK affecting peptide binding. Proc. Natl Acad. Sci. USA, 93, 10632-10637
4. Cho,Y., Gorina,S., Jeffrey,P.D. and Pavletich,N.P. (1994) Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science, 265, 346-355.
5. Chou,P.Y. and Fasman,G.D. (1974) Prediction of protein conformation. Biochemistry, 13, 222-234.
6. Clarke,C.F., Cheng,K., Frey,A.B., Stein,R., Hinds,P.W. and Levine,A.J. (1988) Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: in vitro dissociation of hsc70 and DnaK from murine p53 by ATP. Mol. Cell. Biol., 8, 1206-1215.
7. Conti,E., Franks,N.P. and Brick,P. (1996) Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure, 4, 287-298.
8. Flynn,G.C., Chappell,T.G. and Rothman,J.E. (1989) Peptide binding and release by proteins implicated as catalysts of protein assembly. Science, 245, 385-390.
9. Flynn,G.C., Pohl,J., Flocco,M.T. and Rothman,J.E. (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature, 353, 726-730.
10. Fourie,A.M., Sambrook,J.F. and Gething,M.-J.H. (1994) Common and divergent peptide binding specificities of Hsp70 molecular chaperones. J. Biol. Chem., 269, 30470-30478.
11. Frank,R. (1992) Spot synthesis: an easy technique for positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron, 48, 9217-9232.
12. Gething,M.-J.H. and Sambrook,J.F. (1992) Protein folding in the cell. Nature (Lond.), 355, 33-45.
13. Gragerov,A. and Gottesman,M.E. (1994) Different peptide binding specificities of Hsp70 family members. J. Mol. Biol., 241, 133-135.
14. Gragerov,A., Zeng,L., Zhao,X., Burkholder,W. and Gottesman,M.E. (1994) Specificity of DnaK-peptide binding. J. Mol. Biol., 235, 848-854.
15. Hua,Q.X., Shoelson,S.E., Kochoyan,M. and Weiss,M.A. (1991) Receptor binding redefined by a structural switch in a mutant human insulin. Nature, 354, 238-241.
16. Jeffrey,P.D., Gorina,S. and Pavletich,N.P. (1995) Crystal structure of the tetramerisation domain of the p53 tumor suppressor at 1.7 Angstroms. Science, 267, 1498-1501.
17. Kim,E.E. and Wyckoff,H.W. (1991) Reaction mechanism of alkaline phosphatase based on crystal structures. J. Mol. Biol., 218, 449-464.
18. Klapper,M.H. (1977) The independent distribution of amino acid near neighbor pairs into polypeptides. Biochem. Biophys. Res. Commun., 78, 1018-1024.
19. Kramer,A. and Schneider-Mergener,J. (1997) Synthesis and screening of peptide libraries on continuous cellulose membrane supports. Methods Mol. Biol., in press.
20. Kramer,A., Schuster,A., Reineke,U., Malin,R., Volkmer-Engert,R., Landgraf,C. and Schneider-Mergener,J. (1994) Combinatorial cellulose-bound peptide libraries: screening tools for the identification of peptides that bind ligands with predefined specificity. Methods Companion Methods Enzymol., 6, 388-395.
21. Kramer,A., Vakalopoulou,E., Schleuning,W.-D. and Schneider-Mergener,J. (1995) A general route to fingerprint analyses of peptide-antibody interactions using a clustered amino acid peptide library: comparison with a phage display library. Mol. Immunol., 32, 459-465.
22. Landry,S.J., Jordan,R., McMacken,R. and Gierasch,L.M. (1992) Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature, 355, 455-457.
23. McCarty,J.S., Buchberger,A., Reinstein,J. and Bukau,B. (1995) The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol., 249, 126-137.
24. 32, constiutes a DnaK binding site and is conserved among eubacteria. J. Mol. Biol., 256, 829-837.
25. Morimoto,R.I., Tissieres,A. and Georgopoulos,C. (1994) The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
26. Reineke,U., Sabat,R., Kramer,A., Stigler,R.-D., Seifert,M., Michel,T., Volk,H. and Schneider-Mergener,J. (1995) Mapping protein-protein contact sites using cellulose-bound peptide scans; Mol. Diversity, 1, 141-148.
27. Rüdiger,S., Buchberger,A. and Bukau,B. (1997) Principles governing the interactions of Hsp70 chaperones with substrates. Nature Struct. Biol., in press.
28. Schatz,G. and Dobberstein,B. (1996) Common principles of protein translocation across membranes. Science, 271, 1519-1526.
29. Schultz,S.C., Shields,G.C. and Steitz,T.A. (1991) Crystal structure of a CAP-DNA complex: the DNA is bent by 90°. Science, 253, 1001-1007.
30. 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.
31. Wilson,I.A., Skehel,J.J. and Wiley,D.C. (1981) Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature, 289, 366-373.
32. Zhu,X., Zhao,X., Burkholder,W.F., Gragerov,A., Ogata,C.M., Gottesman,M. and Hendrickson,W.A. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science, 272, 1606-1614.