The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain

Several reader domain proteins that specifically recognize methyllysine-containing histones contain the negatively-charged aspartate or glutamate residues as part of the aromatic cage. Herein, we report thermodynamic analyses for the recognition of histone H3K4me3 and H3K4me2 by the tandem tudor dom...

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Autores principales: Pieters, Bas J. G. E., Meulenbroeks, Erik, Belle, Roman, Mecinović, Jasmin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4589357/
https://www.ncbi.nlm.nih.gov/pubmed/26421618
http://dx.doi.org/10.1371/journal.pone.0139205
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author Pieters, Bas J. G. E.
Meulenbroeks, Erik
Belle, Roman
Mecinović, Jasmin
author_facet Pieters, Bas J. G. E.
Meulenbroeks, Erik
Belle, Roman
Mecinović, Jasmin
author_sort Pieters, Bas J. G. E.
collection PubMed
description Several reader domain proteins that specifically recognize methyllysine-containing histones contain the negatively-charged aspartate or glutamate residues as part of the aromatic cage. Herein, we report thermodynamic analyses for the recognition of histone H3K4me3 and H3K4me2 by the tandem tudor domain of Sgf29 and its recognition site variants. Small uncharged and large aromatic substitutions on the Asp266 site resulted in a significant decrease in binding affinities for both H3K4me3 and H3K4me2, demonstrating the role of the negative charge of Asp266 in the readout process by Sgf29. This study emphasizes the essential contribution of electrostatic interactions to the overall binding affinity, and reveals that the underlying mechanisms for the recognition of Kme2/3 depend on the composition and arrangement of the aromatic cage.
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spelling pubmed-45893572015-10-02 The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain Pieters, Bas J. G. E. Meulenbroeks, Erik Belle, Roman Mecinović, Jasmin PLoS One Research Article Several reader domain proteins that specifically recognize methyllysine-containing histones contain the negatively-charged aspartate or glutamate residues as part of the aromatic cage. Herein, we report thermodynamic analyses for the recognition of histone H3K4me3 and H3K4me2 by the tandem tudor domain of Sgf29 and its recognition site variants. Small uncharged and large aromatic substitutions on the Asp266 site resulted in a significant decrease in binding affinities for both H3K4me3 and H3K4me2, demonstrating the role of the negative charge of Asp266 in the readout process by Sgf29. This study emphasizes the essential contribution of electrostatic interactions to the overall binding affinity, and reveals that the underlying mechanisms for the recognition of Kme2/3 depend on the composition and arrangement of the aromatic cage. Public Library of Science 2015-09-30 /pmc/articles/PMC4589357/ /pubmed/26421618 http://dx.doi.org/10.1371/journal.pone.0139205 Text en © 2015 Pieters et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Pieters, Bas J. G. E.
Meulenbroeks, Erik
Belle, Roman
Mecinović, Jasmin
The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain
title The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain
title_full The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain
title_fullStr The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain
title_full_unstemmed The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain
title_short The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain
title_sort role of electrostatic interactions in binding of histone h3k4me2/3 to the sgf29 tandem tudor domain
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4589357/
https://www.ncbi.nlm.nih.gov/pubmed/26421618
http://dx.doi.org/10.1371/journal.pone.0139205
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