Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini.

ABSTRACT: Individual posttranslational modifications (PTMs) on histones have well established roles in certain biological processes, notably transcriptional programming. Recent genomewide studies describe patterns of covalent modifications, such as H3 methylation and acetylation at promoters of specific target genes, or "bivalent domains," in stem cells, suggestive of a possible combinatorial interplay between PTMs on the same histone. However, detection of long-range PTM associations is often problematic in antibody-based or traditional mass spectrometric-based analyses. Here, histone H3 from a ciliate model was analyzed as an enriched source of transcriptionally active chromatin. Using a recently developed mass spectrometric approach, combinatorial modification states on single, long N-terminal H3

SUBMITTER: Taverna SD 

PROVIDER: S-EPMC1892956 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature