The Effect of the Length of Histone H3K4me3 on Recognition by Reader Proteins

被引：7
|
作者：
Pieters, Bas [1 ]
Belle, Roman [1 ]
Mecinovic, Jasmin [1 ]
机构：
[1] Radboud Univ Nijmegen, Inst Mol & Mat, NL-6525 AJ Nijmegen, Netherlands
来源：
CHEMBIOCHEM | 2013年 / 14卷 / 18期
关键词：
histone; isothermal titration calorimetry; molecular recognition; protein-protein interactions; trimethyllysine; METHYLATION; H3;
D O I：
10.1002/cbic.201300525
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Thermodynamic analyses of associations between reader domain proteins and histone H3K4me3 peptides demonstrated that the shortest recognised histone substrate contains just the first four amino acids in histone 3. Deletion or addition at the N terminus resulted in a substantial decrease of binding affinity for most readers, thus verifying the importance of the H3A1 binding pocket. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码：2408 / 2412
页数：5
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