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Titolo:
ATP BINDING AND HYDROLYSIS ARE ESSENTIAL TO THE FUNCTION OF THE HSP90MOLECULAR CHAPERONE IN-VIVO
Autore:
PANARETOU B; PRODROMOU C; ROE SM; OBRIEN R; LADBURY JE; PIPER PW; PEARL LH;
Indirizzi:
UNIV COLL LONDON,DEPT BIOCHEM & MOL BIOL,GOWER ST LONDON WC1E 6BT ENGLAND UNIV COLL LONDON,DEPT BIOCHEM & MOL BIOL LONDON WC1E 6BT ENGLAND
Titolo Testata:
EMBO journal (Print)
fascicolo: 16, volume: 17, anno: 1998,
pagine: 4829 - 4836
SICI:
0261-4189(1998)17:16<4829:ABAHAE>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEAT-SHOCK PROTEIN; AMINO-TERMINAL DOMAIN; GLUCOCORTICOID RECEPTOR; PROGESTERONE-RECEPTOR; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; TYROSINE KINASE; DNA GYRASE; IN-VIVO; GELDANAMYCIN;
Keywords:
ATP; CHAPERONE; HSP90; PROTEIN FOLDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
68
Recensione:
Indirizzi per estratti:
Citazione:
B. Panaretou et al., "ATP BINDING AND HYDROLYSIS ARE ESSENTIAL TO THE FUNCTION OF THE HSP90MOLECULAR CHAPERONE IN-VIVO", EMBO journal (Print), 17(16), 1998, pp. 4829-4836

Abstract

Hsp90 is an abundant molecular chaperone essential to the establishment of many cellular regulation and signal transduction systems, but remains one of the least well described chaperones. The biochemical mechanism of protein folding by Hsp90 is poorly understood, and the directinvolvement of ATP has been particularly contentious. Here we demonstrate in vitro an inherent ATPase activity in both yeast Hsp90 and the Escherichia coil homologue HtpG, which is sensitive to inhibition by the Hsp90-specific antibiotic geldanamycin. Mutations of residues implicated in ATP binding and hydrolysis by structural studies abolish thisATPase activity in vitro and disrupt Hsp90 function in vivo. These results show that Hsp90 is directly ATP dependent in vivo, and suggest an ATP-coupled chaperone cycle for Hsp90-mediated protein folding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 11:58:20