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- W3190454161 abstract "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." @default.
- W3190454161 created "2021-08-16" @default.
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- W3190454161 date "2021-08-05" @default.
- W3190454161 modified "2023-10-15" @default.
- W3190454161 title "Interactome of Site-Specifically Acetylated Linker Histone H1" @default.
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- W3190454161 doi "https://doi.org/10.1021/acs.jproteome.1c00396" @default.
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