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...

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Autores: Hintzen, Jordi C. J., Poater i Teixidor, Jordi, Kumar, Kiran, Al Temimi, Abbas H. K., Pieters, Bas J. G. E., Paton, Robert S., Bickelhaupt, F. Matthias, Mecinović, Jasmin
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Recursos:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/176149
Acesso em linha:https://hdl.handle.net/2445/176149
Access Level:acceso abierto
Palavra-chave:Epigenètica
Histones
Metilació
Epigenetics
Methylation
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spelling Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader ProteinsHintzen, Jordi C. J.Poater i Teixidor, JordiKumar, KiranAl Temimi, Abbas H. K.Pieters, Bas J. G. E.Paton, Robert S.Bickelhaupt, F. MatthiasMecinović, JasminEpigenèticaHistonesMetilacióEpigeneticsHistonesMethylationGaining 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.MDPI2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/176149Articles publicats en revistes (Química Inorgànica i Orgànica)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.3390/molecules25081918Molecules, 2020, vol. 25, num. 8, p. 1918https://doi.org/10.3390/molecules25081918info:eu-repo/grantAgreement/EC/H2020/715691cc-by (c) Hintzen, Jordi C. J. et al., 2020http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1761492026-05-27T06:46:51Z
dc.title.none.fl_str_mv 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
spellingShingle Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins
Hintzen, Jordi C. J.
Epigenètica
Histones
Metilació
Epigenetics
Histones
Methylation
title_short 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_sort Comparison of Molecular Recognition of Trimethyllysine and Trimethylthialysine by Epigenetic Reader Proteins
dc.creator.none.fl_str_mv Hintzen, Jordi C. J.
Poater i Teixidor, Jordi
Kumar, Kiran
Al Temimi, Abbas H. K.
Pieters, Bas J. G. E.
Paton, Robert S.
Bickelhaupt, F. Matthias
Mecinović, Jasmin
author Hintzen, Jordi C. J.
author_facet Hintzen, Jordi C. J.
Poater i Teixidor, Jordi
Kumar, Kiran
Al Temimi, Abbas H. K.
Pieters, Bas J. G. E.
Paton, Robert S.
Bickelhaupt, F. Matthias
Mecinović, Jasmin
author_role author
author2 Poater i Teixidor, Jordi
Kumar, Kiran
Al Temimi, Abbas H. K.
Pieters, Bas J. G. E.
Paton, Robert S.
Bickelhaupt, F. Matthias
Mecinović, Jasmin
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Epigenètica
Histones
Metilació
Epigenetics
Histones
Methylation
topic Epigenètica
Histones
Metilació
Epigenetics
Histones
Methylation
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.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/176149
url https://hdl.handle.net/2445/176149
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/molecules25081918
Molecules, 2020, vol. 25, num. 8, p. 1918
https://doi.org/10.3390/molecules25081918
info:eu-repo/grantAgreement/EC/H2020/715691
dc.rights.none.fl_str_mv cc-by (c) Hintzen, Jordi C. J. et al., 2020
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Hintzen, Jordi C. J. et al., 2020
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Química Inorgànica i Orgànica)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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