Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain.

doi:10.1016/j.molcel.2016.03.028

Article

Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain.

Molecular cell - 21 Apr 2016

Li Yuanyuan, Sabari Benjamin R, Panchenko Tatyana, Wen Hong, Zhao Dan, Guan Haipeng, Wan Liling, Huang He, Tang Zhanyun, Zhao Yingming, Roeder Robert G, Shi Xiaobing, Allis C David, Li Haitao

Abstract excerpt

Recognition of histone covalent modifications by chromatin-binding protein modules ("readers") constitutes a major mechanism for epigenetic regulation, typified by bromodomains that bind acetyllysine. Non-acetyl histone lysine acylations (e.g., crotonylation, butyrylation, propionylation) have been recently identified, but readers that prefer these acylations have not been characterized. Here we report that the...

Topics

Acetylation
Animals
Binding Sites
Chromatin Assembly and Disassembly
Crotonates
Epigenesis, Genetic
HEK293 Cells
Histones
Humans
Hydrophobic and Hydrophilic Interactions

Lysine

Mice

Models, Molecular

Mutation

Nuclear Proteins

Protein Domains

Protein Processing, Post-Translational

RAW 264.7 Cells

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