In vitro evidence that hsp90 contains two independent chaperone sites

FEBS Letters

Young, Jason C¹  Hartl, F.Ulrich¹  Schneider, Christine¹ 

[1] Cellular Biochemistry, Max-Planck-Institut fur Biochemie, Am Klopferspitz 18A, 82152 Martinsried, Germany

关键词: Hsp90;    Molecular chaperone;    Geldanamycin;    Human;   

DOI  :  10.1016/S0014-5793(97)01363-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hsp90 is an abundant and constitutively expressed stress protein and molecular chaperone. Here we dissected human hsp90 into three major domains to identify the putative chaperone site at which hsp90 binds unfolded polypeptide. Surprisingly, both the N-terminal and the C-terminal domain of hsp90 prevent the aggregation of denatured polypeptides. The chaperone activity of the N-domain is inhibited by geldanamycin, a specific inhibitor of hsp90-mediated protein refolding. While both domains suppress protein aggregation, only the C-domain binds an antigenic peptide derived from VSV G. Based on these results, hsp90 may be the first chaperone to contain two independent chaperone sites with differential specificity.

【 授权许可】

Unknown