期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 31, 页码 8918-8922出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201603106
关键词
epigenetics; GlcNAcylation; nucleosomes; protein modifications; synthetic biology
资金
- Felix Scholarship Foundation
- EPSRC/Cancer Research UK [NS/A000004/1]
- Royal Society Wolfson Research Merit Award
Transcriptional regulation can be established by various post-translational modifications (PTMs) on histone proteins in the nucleosome and by nucleobase modifications on chromosomal DNA. Functional consequences of histone O-GlcNAcylation (O-GlcNAc=O-linked beta-N-acetylglucosamine) are largely unexplored. Herein, we generate homogeneously GlcNAcylated histones and nucleosomes by chemical post-translational modification. Mass-spectrometry-based quantitative interaction proteomics reveals a direct interaction between GlcNAcylated nucleosomes and the facilitates chromatin transcription (FACT) complex. Preferential binding of FACT to GlcNAcylated nucleosomes may point towards O-GlcNAcylation as one of the triggers for FACT-driven transcriptional control.
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