Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2.

ABSTRACT: Post-translational modifications (PTMs) of histones have fundamental effects on chromatin structure and function. While the impact of PTMs on the function of core histones are increasingly well understood, this is much less the case for modifications of linker histone H1, which is at least in part due to a lack of proper tools. In this work, we establish the assembly of intact chromatosomes containing site-specifically ubiquitylated and acetylated linker histone H1.2 variants obtained by a combination of chemical biology approaches. We then use these complexes in a tailored affinity enrichment mass spectrometry workflow to identify and comprehensively characterize chromatosome-specific cellular interactomes and the impact of site-specific linker histone modifications on a proteome-wide sca

SUBMITTER: Saumer P 

PROVIDER: S-EPMC10783519 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature