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Titolo:
Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
Autore:
Prodromou, C; Siligardi, G; OBrien, R; Woolfson, DN; Regan, L; Panaretou, B; Ladbury, JE; Piper, PW; Pearl, LH;
Indirizzi:
Univ Coll London, Dept Biochem & Mol Biol, London WC1E 6BT, England Univ Coll London London England WC1E 6BT Biol, London WC1E 6BT, England UnivX,ondon Kings Coll, Dept Pharm, Pharmaceut Opt Spect Ctr, London SW3 6L Univ London Kings Coll London England SW3 6LX t Spect Ctr, London SW3 6L Univglandex, Sch Biol Sci, Ctr Biomol Design & Drug Dev, Falmer BN1 3FS, En Univ Sussex Falmer England BN1 3FS Design & Drug Dev, Falmer BN1 3FS, En
Titolo Testata:
EMBO JOURNAL
fascicolo: 3, volume: 18, anno: 1999,
pagine: 754 - 762
SICI:
0261-4189(19990201)18:3<754:ROHAAB>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEAT-SHOCK PROTEINS; AMINO-TERMINAL DOMAIN; GLUCOCORTICOID RECEPTOR; PROGESTERONE-RECEPTOR; MOLECULAR CHAPERONE; IN-VIVO; FK506-BINDING IMMUNOPHILIN; CRYSTAL-STRUCTURE; STEROID-RECEPTOR; MUTATED P53;
Keywords:
ATP; chaperone; Hsp90; protein folding; TPR domain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Pearl, LH Univndoll London, Dept Biochem & Mol Biol, Gower St, London WC1E6BT, Engla Univ Coll London Gower St London England WC1E 6BT 1E 6BT, Engla
Citazione:
C. Prodromou et al., "Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones", EMBO J, 18(3), 1999, pp. 754-762

Abstract

The in vivo function of the heat shock protein 90 (Hsp90) molecular chaperone is dependent on the binding and hydrolysis of ATP, and on interactions with a variety of co-chaperones containing tetratricopeptide repeat (TPR) domains. We have now analysed the interaction of the yeast TPR-domain co-chaperones Sti1 and Cpr6 crith yeast Hsp90 by isothermal titration calorimetry, circular dichroism spectroscopy and analytical ultracentrifugation, and determined the effect of their binding on the inherent ATPase activity of Hsp90, Sti1 and Cpr6 both bind with sub-micromolar affinity, with Sti1 binding accompanied by a large conformational change. Two co-chaperone molecules bind per Hsp90 dimer, and Sti1 itself is found to be a dimer in free solution. The inherent ATPase activity of Hsp90 is completely inhibited by binding of Sti1, but is not affected by Cpr6, although Cpr6 can reactivate the ATPase activity by displacing Sti1 from Hsp90, Bound Sti1 makes direct contact with, and blocks access to the ATP-binding site in the N-terminal domain of Hsp90, These results reveal an important role for TPR-domain co-chaperones as regulators of the ATPase activity of Hsp90, showing that the ATP-dependent step in Hsp90-mediated protein folding occurs after the binding of the folding client protein, and suggesting that ATP hydrolysis triggers client-protein release.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 11:27:54