Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex.
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 β-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.
Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, UK.
Ritu
R
Raj
Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, UK.
Lukas
L
Lercher
Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, UK.
Shabaz
S
Mohammed
Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, UK. ben.davis@chem.ox.ac.uk.
Benjamin G
0000-0002-5056-407X
BG
Davis
D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism*; D002843:Chromatin / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D008958:Models, Molecular; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D002843:Chromatin; D009707:Nucleosomes; D000117:Acetylglucosamine
GlcNAcylation; epigenetics; nucleosomes; protein modifications; synthetic biology