Histone H3 N-terminal recognition by the PHD finger of PHRF1 is required for proper DNA damage response.

ABSTRACT: Plant homeodomain (PHD) fingers are critical effectors of histone post-translational modifications (PTMs), acting as regulators of gene expression and genome integrity, and frequently presenting in human disease. While most PHD fingers recognize unmodified and methylated states of histone H3 lysine 4 (H3K4), the specific functions of many of the over 100 PHD finger-containing proteins in humans remain poorly understood, despite their significant implications in disease processes. In this study, we undertook a comprehensive analysis of one such poorly characterized PHD finger-containing protein, PHRF1. Using biochemical, molecular, and cellular approaches, we show that PHRF1 robustly binds to histone H3, specifically at its N-terminal region. Through RNA-seq and proteomic analyses, we also

SUBMITTER: Jain K 

PROVIDER: S-EPMC11601626 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature