Decoding chromatin states by proteomic profiling of nucleosome readers.

ABSTRACT: DNA and histone modifications combine into characteristic patterns that demarcate functional regions of the genome^1,2. While many 'readers' of individual modifications have been described^3-5, how chromatin states comprising composite modification signatures, histone variants and internucleosomal linker DNA are interpreted is a major open question. Here we use a multidimensional proteomics strategy to systematically examine the interaction of around 2,000 nuclear proteins with over 80 modified dinucleosomes representing promoter, enhancer and heterochromatin states. By deconvoluting complex nucleosome-binding profiles into networks of co-regulated proteins and distinct nucleosomal features driving protein recruitment or exclusion, we show comprehensively how chromatin

SUBMITTER: Lukauskas S 

PROVIDER: S-EPMC10954555 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature