Abstract

Histone post‐translational modifications (PTMs) recruit effector molecules to chromatin, which in‐turn regulate DNA‐templated processes including replication, gene expression, and DNA repair. Many recent reports have highlighted the importance of combinatorial PTMs, on one or more histone tail, for coordinating the binding of protein factors. However, the patterns of PTMs that might exist within a nucleosome are still not well understood. Lysine methylation on histone H3 is known to recruit both lysine acetyltransferases and deacetylases to chromatin. In this study, we examined what overlap exists between lysine methylation and acetylation on all four histones within a single nucleosome in budding yeast. Variant combinations of modifications found suggest recruitment of effector molecules is dictated by interaction with more than one histone within a nucleosome.

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