Non-histone binding functions of PHD fingers

Nitika Gaurav; Tatiana G Kutateladze

doi:10.1016/j.tibs.2023.03.005

Non-histone binding functions of PHD fingers

Trends Biochem Sci. 2023 Jul;48(7):610-617. doi: 10.1016/j.tibs.2023.03.005. Epub 2023 Apr 14.

Authors

Nitika Gaurav¹, Tatiana G Kutateladze²

Affiliations

¹ Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
² Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA. Electronic address: tatiana.kutateladze@cuanschutz.edu.

PMID: 37061424
PMCID: PMC10330121 (available on 2024-07-01)
DOI: 10.1016/j.tibs.2023.03.005

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.

Keywords: DNA; PHD; binding mechanism; histone.

Publication types

Review

MeSH terms

DNA-Binding Proteins* / metabolism
Histones / metabolism
PHD Zinc Fingers*
Plants
Protein Binding

Substances

DNA-Binding Proteins
Histones

Abstract

Publication types

MeSH terms

Substances

Grants and funding