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

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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",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "19",

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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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