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Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

Titelangaben

Scheibel, Thomas ; Weikl, Tina ; Buchner, Johannes:
Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence.
In: Proceedings of the National Academy of Sciences of the United States of America. Bd. 95 (Februar 1998) Heft 4 . - S. 1495-1499.
ISSN 0027-8424

Abstract

The abundant molecular chaperone Hsp90 is a key regulator of protein structure in the cytosol of eukaryotic cells. Although under physiological conditions a specific subset of proteins is substrate for Hsp90, under stress conditions Hsp90 seems to perform more general functions. However, the underlying mechanism of Hsp90 remained enigmatic. Here, we analyzed the function of conserved Hsp90 domains. We show that Hsp90 possesses two chaperone sites located in the N- and C-terminal fragments, respectively. The C-terminal fragment binds to partially folded proteins in an ATP-independent way potentially regulated by cochaperones. The N-terminal domain contains a peptide binding site that seems to bind preferentially peptides longer than 10 amino acids. Peptide dissociation is induced by ATP binding. Furthermore, the antitumor drug geldanamycin both inhibits the weak ATPase of Hsp90 and stimulates peptide release. We propose that the existence of two functionally different chaperone sites together with a substrate-selecting set of cochaperones allows Hsp90 to guide the folding of a subset of target proteins and, at the same time, to exhibit general chaperone functions.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Institutionen der Universität: Fakultäten
Fakultäten > Fakultät für Ingenieurwissenschaften
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien > Lehrstuhl Biomaterialien - Univ.-Prof. Dr. Thomas Scheibel
Profilfelder > Advanced Fields > Neue Materialien
Profilfelder > Advanced Fields > Molekulare Biowissenschaften
Profilfelder > Advanced Fields > Polymer- und Kolloidforschung
Profilfelder > Emerging Fields > Lebensmittel- und Gesundheitswissenschaften
Profilfelder
Profilfelder > Advanced Fields
Profilfelder > Emerging Fields
Titel an der UBT entstanden: Nein
Themengebiete aus DDC: 600 Technik, Medizin, angewandte Wissenschaften
600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften
Eingestellt am: 01 Okt 2015 12:52
Letzte Änderung: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/20056