HspB8 interacts with BAG3 in a "native-like" conformation forming a complex that displays chaperone-like activity.

ABSTRACT: The HspB8-BAG3 complex plays an important role in the protein quality control acting alone or within multi-components complexes. To clarify the mechanism underlying its activity, in this work we used biochemical and biophysical approaches to study the tendency of both proteins to auto-assemble and to form the complex. Solubility and Thioflavin T assays, Fourier transform infrared spectroscopy and atomic force microscopy analyses clearly showed the tendency of HspB8 to self-assemble at high concentration and to form oligomers in a "native-like" conformation; otherwise, BAG3 aggregates poorly. Noteworthy, also HspB8 and BAG3 associate in a "native-like" conformation, forming a stable complex. Furthermore, the high difference between dissociation constant values of HspB8-HspB8 interaction wit

SUBMITTER: Sciandrone B 

PROVIDER: S-EPMC10273338 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature