Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

Literature Information

Publication Date 2018-02-09
DOI 10.1039/C8CC01009A
Impact Factor 6.222
Authors

Abbas H. K. Al Temimi, Roman Belle, Kiran Kumar, Peter Betlem, Bas J. G. E. Pieters, Robert S. Paton, Jasmin Mecinović


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Abstract

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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