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The Effect of the Length of Histone H3K4me3 on Recognition by Reader Proteins
Author(s) -
Pieters Bas,
Belle Roman,
Mecinović Jasmin
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201300525
Subject(s) - h3k4me3 , histone , computational biology , computer science , domain (mathematical analysis) , chemistry , biochemistry , biology , dna , gene , gene expression , mathematics , mathematical analysis , promoter
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.