Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

Abbas H.K. Al Temimi; Roman Belle; Kiran Kumar; Jordi Poater; Peter Betlem; Bas J.G.E. Pieters; Robert S. Paton; F. Matthias Bickelhaupt; Jasmin Mecinović

doi:10.1039/c8cc01009a

Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

Abbas H.K. Al Temimi, Roman Belle, Kiran Kumar, Jordi Poater, Peter Betlem, Bas J.G.E. Pieters, Robert S. Paton, F. Matthias Bickelhaupt, Jasmin Mecinović^*

^*Corresponding author for this work

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Abstract

Histone N^ϵ-lysine methylation is a widespread posttranslational modification that is specifically recognised by a diverse class of N^ϵ-methyllysine binding reader proteins. Combined thermodynamic data, molecular dynamics simulations, and quantum chemical studies reveal that reader proteins efficiently bind trimethylornithine and trimethylhomolysine, the simplest N^ϵ-trimethyllysine analogues that differ in the length of the side chain.

Original language	English
Pages (from-to)	2409-2412
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	19
Early online date	9 Feb 2018
DOIs	https://doi.org/10.1039/c8cc01009a
Publication status	Published - 7 Mar 2018

Funding

This work was supported by the ERC Starting Grant to J. M. (ChemEpigen-715691) and the Netherlands Organization for Scientific Research (NCI-TA 731.015.202). K. K. is supported by a World Bank Education Grant. J. P. thanks the Spanish MINECO (CTQ2016-77558-R).

Funders	Funder number
ERC Starting	ChemEpigen-715691
Netherlands Organization for Scientific Research	NCI-TA 731.015.202
World Bank Education
Horizon 2020 Framework Programme	715691

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Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteinsFinal published version, 1.9 MBLicence: Article 25fa Dutch Copyright Act

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AU - Al Temimi, Abbas H.K.

AU - Belle, Roman

AU - Kumar, Kiran

AU - Poater, Jordi

AU - Betlem, Peter

AU - Pieters, Bas J.G.E.

AU - Paton, Robert S.

AU - Bickelhaupt, F. Matthias

AU - Mecinović, Jasmin

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AB - Histone Nϵ-lysine methylation is a widespread posttranslational modification that is specifically recognised by a diverse class of Nϵ-methyllysine binding reader proteins. Combined thermodynamic data, molecular dynamics simulations, and quantum chemical studies reveal that reader proteins efficiently bind trimethylornithine and trimethylhomolysine, the simplest Nϵ-trimethyllysine analogues that differ in the length of the side chain.

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ER -

Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

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