Non-histone binding functions of PHD fingers
Related Experiment Video
Updated: Aug 2, 2025

Analysis of Histone Antibody Specificity with Peptide Microarrays
Published on: August 1, 2017
Nitika Gaurav1, Tatiana G Kutateladze1
1Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Abstract:
Plant homeodomain (PHD) fingers comprise a large and well-established family of epigenetic readers that recognize histone H3. A typical PHD finger binds to the unmodified or methylated amino-terminal tail of H3. This interaction is highly specific and can be regulated by post-translational modifications (PTMs) in H3 and other domains present in the protein. However, a set of PHD fingers has recently been shown to bind non-histone proteins, H3 mimetics, and DNA. In this review, we highlight the molecular mechanisms by which PHD fingers interact with ligands other than the amino terminus of H3 and discuss similarities and differences in engagement with histone and non-histone binding partners.
Related Concept Videos
Spreading of Chromatin Modifications
Writers
The writer...
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
The Nucleosome Core Particle
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Nucleosome Remodeling
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Inheritance of Chromatin Structures

