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 unexplor...

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Main Authors: Raj, Ritu, Lercher, Lukas, Mohammed, Shabaz, Davis, Benjamin G.
Format: Online
Language:English
Published: John Wiley and Sons Inc. 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5111754/
id pubmed-5111754
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spelling pubmed-51117542016-11-16 Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex Raj, Ritu Lercher, Lukas Mohammed, Shabaz Davis, Benjamin G. Communications 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. John Wiley and Sons Inc. 2016-06-08 2016-07-25 /pmc/articles/PMC5111754/ /pubmed/27272618 http://dx.doi.org/10.1002/anie.201603106 Text en © 2016 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Raj, Ritu
Lercher, Lukas
Mohammed, Shabaz
Davis, Benjamin G.
spellingShingle Raj, Ritu
Lercher, Lukas
Mohammed, Shabaz
Davis, Benjamin G.
Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex
author_facet Raj, Ritu
Lercher, Lukas
Mohammed, Shabaz
Davis, Benjamin G.
author_sort Raj, Ritu
title Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex
title_short Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex
title_full Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex
title_fullStr Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex
title_full_unstemmed Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex
title_sort synthetic nucleosomes reveal that glcnacylation modulates direct interaction with the fact complex
description 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.
publisher John Wiley and Sons Inc.
publishDate 2016
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5111754/
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