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Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins
Gaining a fundamental insight into the biomolecular recognition of posttranslationally modified histones by epigenetic reader proteins is of crucial importance to understanding the regulation of the activity of human genes. Here, we seek to establish whether trimethylthialysine, a simple trimethylly...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7221964/ https://www.ncbi.nlm.nih.gov/pubmed/32326252 http://dx.doi.org/10.3390/molecules25081918 |
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author | Hintzen, Jordi C. J. Poater, Jordi Kumar, Kiran Al Temimi, Abbas H. K. Pieters, Bas J. G. E. Paton, Robert S. Bickelhaupt, F. Matthias Mecinović, Jasmin |
author_facet | Hintzen, Jordi C. J. Poater, Jordi Kumar, Kiran Al Temimi, Abbas H. K. Pieters, Bas J. G. E. Paton, Robert S. Bickelhaupt, F. Matthias Mecinović, Jasmin |
author_sort | Hintzen, Jordi C. J. |
collection | PubMed |
description | Gaining a fundamental insight into the biomolecular recognition of posttranslationally modified histones by epigenetic reader proteins is of crucial importance to understanding the regulation of the activity of human genes. Here, we seek to establish whether trimethylthialysine, a simple trimethyllysine analogue generated through cysteine alkylation, is a good trimethyllysine mimic for studies on molecular recognition by reader proteins. Histone peptides bearing trimethylthialysine and trimethyllysine were examined for binding with five human reader proteins employing a combination of thermodynamic analyses, molecular dynamics simulations and quantum chemical analyses. Collectively, our experimental and computational findings reveal that trimethylthialysine and trimethyllysine exhibit very similar binding characteristics for the association with human reader proteins, thereby justifying the use of trimethylthialysine for studies aimed at dissecting the origin of biomolecular recognition in epigenetic processes that play important roles in human health and disease. |
format | Online Article Text |
id | pubmed-7221964 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-72219642020-05-22 Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins Hintzen, Jordi C. J. Poater, Jordi Kumar, Kiran Al Temimi, Abbas H. K. Pieters, Bas J. G. E. Paton, Robert S. Bickelhaupt, F. Matthias Mecinović, Jasmin Molecules Article Gaining a fundamental insight into the biomolecular recognition of posttranslationally modified histones by epigenetic reader proteins is of crucial importance to understanding the regulation of the activity of human genes. Here, we seek to establish whether trimethylthialysine, a simple trimethyllysine analogue generated through cysteine alkylation, is a good trimethyllysine mimic for studies on molecular recognition by reader proteins. Histone peptides bearing trimethylthialysine and trimethyllysine were examined for binding with five human reader proteins employing a combination of thermodynamic analyses, molecular dynamics simulations and quantum chemical analyses. Collectively, our experimental and computational findings reveal that trimethylthialysine and trimethyllysine exhibit very similar binding characteristics for the association with human reader proteins, thereby justifying the use of trimethylthialysine for studies aimed at dissecting the origin of biomolecular recognition in epigenetic processes that play important roles in human health and disease. MDPI 2020-04-21 /pmc/articles/PMC7221964/ /pubmed/32326252 http://dx.doi.org/10.3390/molecules25081918 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 | Article Hintzen, Jordi C. J. Poater, Jordi Kumar, Kiran Al Temimi, Abbas H. K. Pieters, Bas J. G. E. Paton, Robert S. Bickelhaupt, F. Matthias Mecinović, Jasmin Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins |
title | Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins |
title_full | Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins |
title_fullStr | Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins |
title_full_unstemmed | Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins |
title_short | Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins |
title_sort | comparison of molecular recognition of trimethyllysine and trimethylthialysine by epigenetic reader proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7221964/ https://www.ncbi.nlm.nih.gov/pubmed/32326252 http://dx.doi.org/10.3390/molecules25081918 |
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