Data from: Lysine-14 acetylation of histone H3 in chromatin confers resistance to the deacetylase and demethylase activities of an epigenetic silencing complex

Wu, Mingxuan, Johns Hopkins University School of Medicine

Hayward, Dawn, Johns Hopkins University School of Medicine

Kalin, Jay H., Johns Hopkins University School of Medicine

Song, Yun, University of Leicester

Schwabe, John W.R., University of Leicester

Cole, Philip A., Johns Hopkins University School of Medicine

Schwabe, John WR, University of Leicester

Published Jun 06, 2018 on Dryad. https://doi.org/10.5061/dryad.413tm83

Cite this dataset

Wu, Mingxuan et al. (2018). Data from: Lysine-14 acetylation of histone H3 in chromatin confers resistance to the deacetylase and demethylase activities of an epigenetic silencing complex [Dataset]. Dryad. https://doi.org/10.5061/dryad.413tm83

Abstract

The core CoREST complex (LHC) contains histone deacetylase HDAC1 and histone demethylase LSD1 held together by the scaffold protein CoREST. Here we analyze the purified LHC with modified peptide and reconstituted semisynthetic mononucleosome substrates. LHC demethylase activity toward methyl-Lys4 in histone H3 is strongly inhibited by H3 Lys14 acetylation, and this appears to be an intrinsic property of the LSD1 subunit. Moreover, the deacetylase selectivity of LHC unexpectedly shows a marked preference for H3 acetyl-Lys9 versus acetyl-Lys14 in nucleosome substrates but this selectivity is lost with isolated acetyl-Lys H3 protein. This diminished activity of LHC for Lys14 deacetylation in nucleosomes is not merely due to steric accessibility based on the pattern of sensitivity of the LHC enzymatic complex to hydroxamic acid-mediated inhibition. Overall, these studies have revealed how a single Lys modification can confer a composite of resistance in chromatin to a key epigenetic enzyme complex involved in gene silencing.

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HNMR Raw Data

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HNMR raw data

Data from: Lysine-14 acetylation of histone H3 in chromatin confers resistance to the deacetylase and demethylase activities of an epigenetic silencing complex

Cite this dataset

Abstract

Usage notes

Figure 2A

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