Atypical histone targets of PHD fingers.
Autor: | Black JC; Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA., Kutateladze TG; Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA. Electronic address: tatiana.kutateladze@cuanschutz.edu. |
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Jazyk: | angličtina |
Zdroj: | The Journal of biological chemistry [J Biol Chem] 2023 Apr; Vol. 299 (4), pp. 104601. Date of Electronic Publication: 2023 Mar 11. |
DOI: | 10.1016/j.jbc.2023.104601 |
Abstrakt: | 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. Competing Interests: Conflict of interest The author declares that they have no conflicts of interest with the contents of this article. (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.) |
Databáze: | MEDLINE |
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