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Global profiling of protein-DNA and protein-nucleosome binding affinities using quantitative mass spectrometry.
Nat. Commun. 9:1653 (2018)
Interaction proteomics studies have provided fundamental insights into multimeric biomolecular assemblies and cell-scale molecular networks. Significant recent developments in mass spectrometry-based interaction proteomics have been fueled by rapid advances in label-free, isotopic, and isobaric quantitation workflows. Here, we report a quantitative protein-DNA and protein-nucleosome binding assay that uses affinity purifications from nuclear extracts coupled with isobaric chemical labeling and mass spectrometry to quantify apparent binding affinities proteome-wide. We use this assay with a variety of DNA and nucleosome baits to quantify apparent binding affinities of monomeric and multimeric transcription factors and chromatin remodeling complexes.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Randomized Controlled-trial; Chronic Tic Disorders; Parkinsons-disease; Health-care; Tourette-syndrome; Behavior-therapy; Neurological Disorders; Huntington Disease; Batten-disease; Virtual Visits
ISSN (print) / ISBN
2041-1723
e-ISSN
2041-1723
Journal
Nature Communications
Quellenangaben
Volume: 9,
Issue: 1,
Article Number: 1653
Publisher
Nature Publishing Group
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Functional Epigenetics (IFE)