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

Research output: Contribution to journal › Article › peer-review

14 Citations (Scopus)

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
DOIs	https://doi.org/10.1039/c8cc01009a
Publication status	Published - 2018
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c8cc01009a

Cite this

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title = "Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins",

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.",

author = "\{Al Temimi\}, \{Abbas H.K.\} and Roman Belle and Kiran Kumar and Jordi Poater and Peter Betlem and Pieters, \{Bas J.G.E.\} and Paton, \{Robert S.\} and Bickelhaupt, \{F. Matthias\} and Jasmin Mecinovi{\'c}",

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year = "2018",

doi = "10.1039/c8cc01009a",

language = "English",

volume = "54",

pages = "2409--2412",

journal = "Chemical Communications",

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publisher = "Royal Society of Chemistry",

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TY - JOUR

T1 - Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

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

PY - 2018

Y1 - 2018

N2 - 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.

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.

UR - https://www.scopus.com/pages/publications/85042932408

U2 - 10.1039/c8cc01009a

DO - 10.1039/c8cc01009a

M3 - Article

C2 - 29457186

AN - SCOPUS:85042932408

SN - 1359-7345

VL - 54

SP - 2409

EP - 2412

JO - Chemical Communications

JF - Chemical Communications

IS - 19

ER -

Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

Abstract

ASJC Scopus subject areas

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