Publikation: Interactome of Site-Specifically Acetylated Linker Histone H1
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Linker histone H1 plays a key role in chromatin organization and maintenance, yet our knowledge of the regulation of H1 functions by post-translational modifications is rather limited. In this study, we report on the generation of site-specifically mono- and di-acetylated linker histone H1.2 by genetic code expansion. We used these modified histones to identify and characterize the acetylation-dependent cellular interactome of H1.2 by affinity purification mass spectrometry and show that site-specific acetylation results in overlapping but distinct groups of interacting partners. Among these, we find multiple translational initiation factors and transcriptional regulators such as the NAD+-dependent deacetylase SIRT1, which we demonstrate to act on acetylated H1.2. Taken together, our data suggest that site-specific acetylation of H1.2 plays a role in modulating protein–protein interactions.
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HÖLLMÜLLER, Eva, Katharina GREINER, Simon Maria KIENLE, Martin SCHEFFNER, Andreas MARX, Florian STENGEL, 2021. Interactome of Site-Specifically Acetylated Linker Histone H1. In: Journal of Proteome Research. American Chemical Society (ACS). 2021, 20(9), pp. 4443-4451. ISSN 1535-3893. eISSN 1535-3907. Available under: doi: 10.1021/acs.jproteome.1c00396BibTex
@article{Hollmuller2021-09-03Inter-54975, year={2021}, doi={10.1021/acs.jproteome.1c00396}, title={Interactome of Site-Specifically Acetylated Linker Histone H1}, number={9}, volume={20}, issn={1535-3893}, journal={Journal of Proteome Research}, pages={4443--4451}, author={Höllmüller, Eva and Greiner, Katharina and Kienle, Simon Maria and Scheffner, Martin and Marx, Andreas and Stengel, Florian} }
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