Interaction of Hsp90 with 20S proteasome: thermodynamic and kinetic characterization.
The proteasome and heat shock proteins have been found in the centrosome. The evidence of their copurification reported by several studies suggests that they form stable complex. In addition, Hsp90 is involved in the loading of proteasome-generated antigenic peptides to the class I major histocompatibility complex. In this article, we report a detailed thermodynamic and kinetic characterization of the Hsp90-20S proteasome interaction, using a surface plasmon resonance technique. The modulation exerted by protons in solution has been investigated, and the results have been discussed, taking into account structural motifs characterizing the binding interface between the two macromolecules.
Department of Molecular, Cellular and Animal Biology, University of Camerino, Camerino, MC, Italy.
A M
AM
Eleuteri
M
M
Cuccioloni
J
J
Bellesi
G
G
Lupidi
E
E
Fioretti
M
M
Angeletti
D000818:Animals; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism* / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008956:Models, Chemical; D009097:Multienzyme Complexes / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D020349:Surface Plasmon Resonance; D013816:Thermodynamics
D018841:HSP90 Heat-Shock Proteins; D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex