A Subset of Human Bromodomains Recognizes Butyryllysine and Crotonyllysine Histone Peptide Modifications

Bromodomains are epigenetic readers that are recruited to acetyllysine residues in histone tails. Recent studies have identified non-acetyl acyllysine modifications, raising the possibility that these might be read by bromodomains. Profiling the nearly complete human bromodomain family revealed that...

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Veröffentlicht in:	Structure (London) 2015-10, Vol.23 (10), p.1801-1814
Hauptverfasser:	Flynn, E. Megan, Huang, Oscar W., Poy, Florence, Oppikofer, Mariano, Bellon, Steve F., Tang, Yong, Cochran, Andrea G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acylation Binding Sites Butyrates - chemistry Butyrates - metabolism Crotonates - chemistry Crotonates - metabolism Crystallography, X-Ray Epigenesis, Genetic Escherichia coli - genetics Escherichia coli - metabolism Gene Expression Histone Acetyltransferases - chemistry Histone Acetyltransferases - genetics Histone Acetyltransferases - metabolism Histones - chemistry Histones - genetics Histones - metabolism Humans Kinetics Lysine - chemistry Lysine - metabolism Models, Molecular Protein Array Analysis Protein Binding Protein Processing, Post-Translational Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism TATA-Binding Protein Associated Factors - chemistry TATA-Binding Protein Associated Factors - genetics TATA-Binding Protein Associated Factors - metabolism Transcription Factor TFIID - chemistry Transcription Factor TFIID - genetics Transcription Factor TFIID - metabolism Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism Water - chemistry Water - metabolism
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