ArticleMethods in molecular biology (Clifton, N.J.)2025
A Method for Characterizing Protein-Histone Peptide Interactions In Vitro.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Histone posttranslational modifications (PTMs) contribute to transcriptional regulation and generate in combination a "histone code," which is largely conserved among organismal kingdoms. By binding to specific PTMs, histone reader proteins act as molecular interpreters of the histone code. These proteins play a crucial role in gene regulation and chromatin structure by recruiting other proteins to the chromatin or blocking histone-modifying enzymes from accessing chromatin. Revealing the specificity of histone readers is, therefore, fundamental to understanding their function in gene regulation. Here, we describe a protocol to identify the binding specificity of histone readers to PTMs using histone peptide arrays and in vitro pull-down assays.
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