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The Taf14 YEATS domain is a reader of histone crotonylation
- Source :
- Nature chemical biology
- Publication Year :
- 2016
-
Abstract
- The discovery of new histone modifications is unfolding at startling rates, however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation – an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.
- Subjects :
- 0301 basic medicine
Models, Molecular
Saccharomyces cerevisiae Proteins
PTM
Protein domain
Taf14
Computational biology
histone
Saccharomyces cerevisiae
Biology
Article
Epigenesis, Genetic
Histones
03 medical and health sciences
Protein Domains
Transcription (biology)
Histone code
Epigenetics
Molecular Biology
Molecular Structure
Lysine
crotonylated lysine
YEATS domain
Cell Biology
Molecular biology
030104 developmental biology
Histone
Transcription Factor TFIID
Posttranslational modification
biology.protein
chromatin
Protein Processing, Post-Translational
Subjects
Details
- Language :
- English
- ISSN :
- 15524469 and 15524450
- Volume :
- 12
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Nature chemical biology
- Accession number :
- edsair.doi.dedup.....3ec22fe9730c544d138fc07760c0cf76