Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics

Morgan Bernier, Yi Luo, Kingsley C. Nwokelo, Michelle Goodwin, Sarah J. Dreher, Pei Zhang, Mark R. Parthun, Yvonne Fondufe-Mittendorf, Jennifer J. Ottesen and Michael G. Poirier ()
Additional contact information
Morgan Bernier: The Ohio State University
Yi Luo: Biophysics Graduate Program, The Ohio State University
Kingsley C. Nwokelo: The Ohio State University
Michelle Goodwin: The Ohio State University
Sarah J. Dreher: The Ohio State Biochemistry Program, The Ohio State University
Pei Zhang: The Ohio State University
Mark R. Parthun: The Ohio State University
Yvonne Fondufe-Mittendorf: University of Kentucky
Jennifer J. Ottesen: Biophysics Graduate Program, The Ohio State University
Michael G. Poirier: The Ohio State University

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: Abstract H1 linker histones are highly abundant proteins that compact nucleosomes and chromatin to regulate DNA accessibility and transcription. However, the mechanisms that target H1 regulation to specific regions of eukaryotic genomes are unknown. Here we report fluorescence measurements of human H1 regulation of nucleosome dynamics and transcription factor (TF) binding within nucleosomes. H1 does not block TF binding, instead it suppresses nucleosome unwrapping to reduce DNA accessibility within H1-bound nucleosomes. We then investigated H1 regulation by H3K56 and H3K122 acetylation, two transcriptional activating histone post translational modifications (PTMs). Only H3K56 acetylation, which increases nucleosome unwrapping, abolishes H1.0 reduction of TF binding. These findings show that nucleosomes remain dynamic, while H1 is bound and H1 dissociation is not required for TF binding within the nucleosome. Furthermore, our H3K56 acetylation measurements suggest that a single-histone PTM can define regions of the genome that are not regulated by H1.

Date: 2015
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DOI: 10.1038/ncomms10152

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