2022 journal article
Modified Histone Peptides Linked to Magnetic Beads Reduce Binding Specificity
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 23(3).
author keywords: yeast surface display; histone post-translational modifications; affinity reagents; protein engineering; chromodomain; binder; reader; antibody; epigenome engineering; synthetic biology
MeSH headings : HEK293 Cells; Histone Code; Histones / metabolism; Humans; Jurkat Cells; K562 Cells; Protein Array Analysis; Protein Binding; Protein Engineering; Protein Processing, Post-Translational; Saccharomyces cerevisiae
TL;DR:
Specific experimental conditions that affect binding specificities of post-translationally modified histones in classic protein engineering platforms are described and likely explain the relative difficulty with histone targets in these platforms.
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Added: February 21, 2022
Histone post-translational modifications are small chemical changes to the histone protein structure that have cascading effects on diverse cellular functions. Detecting histone modifications and characterizing their binding partners are critical steps in understanding chromatin biochemistry and have been accessed using common reagents such as antibodies, recombinant assays, and FRET-based systems. High-throughput platforms could accelerate work in this field, and also could be used to engineer de novo histone affinity reagents; yet, published studies on their use with histones have been noticeably sparse. Here, we describe specific experimental conditions that affect binding specificities of post-translationally modified histones in classic protein engineering platforms and likely explain the relative difficulty with histone targets in these platforms. We also show that manipulating avidity of binding interactions may improve specificity of binding.