{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jacinto MP"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["1388-1393"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10124317"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["62(8)"],"pubmed_abstract":["Treatment of HeLa cells with the DNA damaging agent, bleomycin (BLM), results in the formation of a nonenzymatic 5-methylene-2-pyrrolone histone covalent modification on lysine residues (K<sub>MP</sub>). K<sub>MP</sub> is much more electrophilic than other <i>N</i>-acyllysine covalent modifications and post-translational modifications, including <i>N</i>-acetyllysine (K<sub>Ac</sub>). Using histone peptides containing K<sub>MP</sub>, we show that this modification inhibits the class I histone deacetylase, HDAC1, by reacting with a conserved cysteine (C261) located near the active site. HDAC1 is inhibited by histone peptides whose corresponding <i>N</i>-acetylated sequences are known deacetylation substrates, but not one containing a scrambled sequence. The HDAC1 inhibitor, trichostatin A, "],"journal":["Biochemistry"],"pubmed_title":["Histone Deacetylase 1 Inhibition by Peptides Containing a DNA Damage-Induced, Nonenzymatic, Histone Covalent Modification."],"pmcid":["PMC10124317"],"funding_grant_id":["GM-131736","R35 GM131736"],"pubmed_authors":["Jacinto MP","Greenberg MM"],"additional_accession":[]},"is_claimable":false,"name":"Histone Deacetylase 1 Inhibition by Peptides Containing a DNA Damage-Induced, Nonenzymatic, Histone Covalent Modification.","description":"Treatment of HeLa cells with the DNA damaging agent, bleomycin (BLM), results in the formation of a nonenzymatic 5-methylene-2-pyrrolone histone covalent modification on lysine residues (K<sub>MP</sub>). K<sub>MP</sub> is much more electrophilic than other <i>N</i>-acyllysine covalent modifications and post-translational modifications, including <i>N</i>-acetyllysine (K<sub>Ac</sub>). Using histone peptides containing K<sub>MP</sub>, we show that this modification inhibits the class I histone deacetylase, HDAC1, by reacting with a conserved cysteine (C261) located near the active site. HDAC1 is inhibited by histone peptides whose corresponding <i>N</i>-acetylated sequences are known deacetylation substrates, but not one containing a scrambled sequence. The HDAC1 inhibitor, trichostatin A, ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2026-04-29T14:14:15.613Z","creation":"2025-04-06T00:49:35.649Z"},"accession":"S-EPMC10124317","cross_references":{"pubmed":["36972223"],"doi":["10.1021/acs.biochem.3c00007"]}}