DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues.

ABSTRACT: Histone chaperones are a diverse class of proteins that facilitate chromatin assembly. Their ability to stabilize highly abundant histone proteins in the cellular environment prevents non-specific interactions and promotes nucleosome formation, but the various mechanisms for doing so are not well understood. We now focus on the dynamic features of the DAXX histone chaperone that have been elusive from previous structural studies. Using hydrogen/deuterium exchange coupled to mass spectrometry (H/DX-MS), we elucidate the concerted binding-folding of DAXX with histone variants H3.3/H4 and H3.2/H4 and find that high local stability at the variant-specific recognition residues rationalizes its known selectivity for H3.3. We show that the DAXX histone binding domain is largely disordered in solu

SUBMITTER: DeNizio JE 

PROVIDER: S-EPMC3985662 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature