Issue 20, 2020
From the journal:

Chemical Communications

Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases†

Abbas H. K. Al Temimi, ORCID logo a   Paul B. White, ORCID logo a   Marcus J. M. Mulders,b   Nicole G. A. van der Linden,a   Richard H. Blaauw,c   Anita Wegert,*b   Floris P. J. T. Rutjes ORCID logo *a  and  Jasmin Mecinović ORCID logo *ad  

* Corresponding authors

a Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
E-mail: Floris.Rutjes@ru.nl
Tel: +31 24 3653202

b Mercachem B.V., Kerkenbos 1013, 6546 BB Nijmegen, The Netherlands
E-mail: anita.wegert@mercachem.nl
Tel: +31 24 3652331

c Chiralix B.V., Kerkenbos 1013, 6546 BB Nijmegen, The Netherlands

d University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark
E-mail: mecinovic@sdu.dk
Tel: +45 65 503603

Abstract

We report synthesis and enzymatic assays on human histone lysine methyltransferase catalysed methylation of histones that possess lysine and its geometrically constrained analogues containing rigid (E)-alkene (KE), (Z)-alkene (KZ) and alkyne (Kyne) moieties. Methyltransferases G9a and GLP do have a capacity to catalyse methylation in the order K ≫ KE > KZ ∼ Kyne, whereas monomethyltransferase SETD8 catalyses only methylation of K and KE.

Graphical abstract: Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases

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Article information

DOI
https://doi.org/10.1039/C9CC09098C
Article type
Communication
Submitted
22 Nov 2019
Accepted
03 Feb 2020
First published
03 Feb 2020
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2020,56, 3039-3042

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Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases

A. H. K. Al Temimi, P. B. White, M. J. M. Mulders, N. G. A. van der Linden, R. H. Blaauw, A. Wegert, F. P. J. T. Rutjes and J. Mecinović, Chem. Commun., 2020, 56, 3039 DOI: 10.1039/C9CC09098C

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