Premium
Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex
Author(s) -
Raj Ritu,
Lercher Lukas,
Mohammed Shabaz,
Davis Benjamin G.
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201603106
Subject(s) - histone , nucleosome , chromatin , chemistry , dna , transcription (linguistics) , histone methylation , microbiology and biotechnology , transcriptional regulation , posttranslational modification , computational biology , biophysics , transcription factor , biochemistry , biology , dna methylation , gene , gene expression , enzyme , linguistics , philosophy
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.