Atypical histone targets of PHD fingers.

J Biol Chem

Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA. Electronic address:

Published: April 2023

AI Article Synopsis

  • Plant homeodomain (PHD) fingers are specialized protein structures that bind to certain histone tails, influencing gene expression and DNA repair.
  • Recent studies show that some PHD fingers can also interact with different parts of histones H3 and H4, expanding their functional capabilities.
  • The review explores how these atypical interactions work, their biological significance, potential for therapy, and methods to inhibit their activity.

Article Abstract

Plant homeodomain (PHD) fingers are structurally conserved zinc fingers that selectively bind unmodified or methylated at lysine 4 histone H3 tails. This binding stabilizes transcription factors and chromatin-modifying proteins at specific genomic sites, which is required for vital cellular processes, including gene expression and DNA repair. Several PHD fingers have recently been shown to recognize other regions of H3 or histone H4. In this review, we detail molecular mechanisms and structural features of the noncanonical histone recognition, discuss biological implications of the atypical interactions, highlight therapeutic potential of PHD fingers, and compare inhibition strategies.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10124903PMC
http://dx.doi.org/10.1016/j.jbc.2023.104601DOI Listing

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