Cargando…

Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark

The five members of the family of tumor suppressors ING contain a Plant Homeodomain (PHD) that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) with an affinity in the low micromolar range. Here, we use NMR to show that in the presence of 15% Ficoll 70, an inert macromolecular...

Descripción completa

Detalles Bibliográficos
Autores principales: Palacios, Alicia, Blanco, Francisco J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7072245/
https://www.ncbi.nlm.nih.gov/pubmed/32033221
http://dx.doi.org/10.3390/biom10020234
_version_ 1783506361599918080
author Palacios, Alicia
Blanco, Francisco J
author_facet Palacios, Alicia
Blanco, Francisco J
author_sort Palacios, Alicia
collection PubMed
description The five members of the family of tumor suppressors ING contain a Plant Homeodomain (PHD) that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) with an affinity in the low micromolar range. Here, we use NMR to show that in the presence of 15% Ficoll 70, an inert macromolecular crowding agent, the mode of binding does not change but the affinity increases by one order of magnitude. The affinity increases also for unmethylated histone H3 tail, but the difference with H3K4me3 is larger in the presence of Ficoll. These results indicate that in the cellular milieu, the affinity of the ING proteins for their chromatin target is larger than previously thought.
format Online
Article
Text
id pubmed-7072245
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-70722452020-03-19 Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark Palacios, Alicia Blanco, Francisco J Biomolecules Communication The five members of the family of tumor suppressors ING contain a Plant Homeodomain (PHD) that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) with an affinity in the low micromolar range. Here, we use NMR to show that in the presence of 15% Ficoll 70, an inert macromolecular crowding agent, the mode of binding does not change but the affinity increases by one order of magnitude. The affinity increases also for unmethylated histone H3 tail, but the difference with H3K4me3 is larger in the presence of Ficoll. These results indicate that in the cellular milieu, the affinity of the ING proteins for their chromatin target is larger than previously thought. MDPI 2020-02-04 /pmc/articles/PMC7072245/ /pubmed/32033221 http://dx.doi.org/10.3390/biom10020234 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Palacios, Alicia
Blanco, Francisco J
Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark
title Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark
title_full Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark
title_fullStr Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark
title_full_unstemmed Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark
title_short Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark
title_sort macromolecular crowding increases the affinity of the phd of ing4 for the histone h3k4me3 mark
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7072245/
https://www.ncbi.nlm.nih.gov/pubmed/32033221
http://dx.doi.org/10.3390/biom10020234
work_keys_str_mv AT palaciosalicia macromolecularcrowdingincreasestheaffinityofthephdofing4forthehistoneh3k4me3mark
AT blancofranciscoj macromolecularcrowdingincreasestheaffinityofthephdofing4forthehistoneh3k4me3mark