Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90

Katarzyna M. Tych, Markus Jahn, Florian Gegenfurtner, Vera K. Hechtl, Johannes Buchner, Thorsten Hugel, Matthias Rief*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

5 Citaten (Scopus)


Hsp90 is an essential molecular chaperone, which has to be in a dimeric form for its correct function. While the affinity of the dimer has previously been measured, little is known about how it associates and dissociates and the factors that influence this. We perform an in-depth single molecule characterization of the C-terminal association and dissociation of Hsp90. We find more than one dissociation rate, indicating that the dimer has a stable and an unstable state. Furthermore, we find that the stability of the C-terminal association is dependent on the presence of ATP, despite the C-terminal dimerization interface being distal to the catalytic site.

Originele taal-2English
Pagina's (van-tot)11373-11380
Aantal pagina's8
TijdschriftJournal of Physical Chemistry B
Nummer van het tijdschrift49
StatusPublished - 13-dec-2018
Extern gepubliceerdJa

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