Molecular chaperones: Clasping the prize

Current Biology

Volumn 6, Issue 12, 1996, Pages 1573-1576

  Gething, Mary Jane ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 0030480940     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(02)70775-6     Document Type: Review

References (19)

1. Gething MJ, Sambrook JF: Protein folding in the cell. Nature 1992, 355:33-45.
2. Boorstein WR, Ziegelhoffer T, Craig EA: Molecular evolution of the HSP70 multigene family. J Mol Evol 1994, 38:1-17.
3. Becker J, Craig EA: Heat-shock proteins as molecular chaperones. Eur J Biochem 1994, 219:11-23.
4. Hartl FU: Molecular chaperones in cellular protein folding. Nature 1996, 381:571-580.
5. Flynn GC, Pohl J, Flocco MT, Rothman JE: Peptide-binding specificity of the molecular chaperone BiP. Nature 1991, 353:726-730.
6. Blond-Elguindi S, Cwirla SE, Dower WJ, Lipshutz RJ, Sprang SR, Sambrook JF, Gething MJ: Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 1993, 75:717-728.
7. Gragerov A, Zeng L, Zhao X, Burkholder W, Gottesman ME: Specificity of DnaK-peptide binding. J Mol Biol 1994, 235:848-854.
8. McKay DB: Structure and mechanism of 70-kDa heat-shock-related proteins. Adv Prot Chem 1993, 44:67-80.
9. Flaherty KM, DeLuca-Flaherty C, McKay DB: Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 1990, 346:623-628.
10. Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA: Structural analysis of substrate binding by the molecular chaperone DnaK. Science 1996, 272:1606-1614.
11. Takenaka IM, Leung S-M, McAndrew SJ, Brown JP, Hightower LE: Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences. J Biol Chem 1995, 270:19839-19844.
12. Fourie AM, Sambrook JF, Gething M-JH: Common and divergent peptide-binding specificities of hsp70 molecular chaperones. J Biol Chem 1994, 269:30470-30478.
13. Gragerov A, Gottesman ME: Different peptide binding specificities of hsp70 family members. J Mol Biol 1994, 241:133-135.
14. Morshauser RC, Wang H, Flynn GC, Zuiderweg ERP: The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology. Biochemistry 1995, 34:6261-6266.
15. Noel JP, Hamm HE, Sigler PB: The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 1993, 366:654-663.
16. iα1 and the mechanism of GTP hydrolysis. Science 1994, 265:1405-1412.
17. Fung KL, Hilgenberg L, Wang N, Chirico WJ: Conformations of the nucleotide and polypeptide binding domains of cytosolic Hsp70 molecular chaperones are coupled. J Biol Chem 1996, 271:21559-21565.
18. Wawrzynów A, Zylicz M: 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 1995, 270:19300-19306.
19. Knarr G, Gething M-J, Modrow S, Buchner J: BiP-binding sequences in antibodies. J Biol Chem 1995, 270:27589-27594.