ArticleNucleic acids research2006
Developmental activation of the lysozyme gene in chicken macrophage cells is linked to core histone acetylation at its enhancer elements.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Chromatin profiling in human neurons reveals aberrant roles for histone acetylation and BET family proteins in schizophrenia.Nature communications · 2022Article
- Article
- The histone variant H2A.Z in gene regulation.Epigenetics & chromatin · 2019Review
- Histone variant H2A.Z deposition and acetylation directs the canonical Notch signaling response.Nucleic acids research · 2018Article
- FANCJ coordinates two pathways that maintain epigenetic stability at G-quadruplex DNA.Nucleic acids research · 2012Article
- Article
- Epigenetic instability due to defective replication of structured DNA.Molecular cell · 2010Article
- Acetylation of vertebrate H2A.Z and its effect on the structure of the nucleosome.Biochemistry · 2009Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Native chromatin IP assays were used to define changes in core histone acetylation at the lysozyme locus during developmental maturation of chicken macrophages and stimulation to high-level expression by lipo-polysaccharide. In pluripotent precursors the lysozyme gene (Lys) is inactive and there is no acetylation of core histones at the gene, its promoter or at the upstream cis-control elements. In myeloblasts, where there is a very low level of Lys expression, H4 acetylation appears at the cis-control elements but not at the Lys gene or its promoter: neither H3 nor H2B become significantly acetylated in myeloblasts. In mature macrophages, Lys expression increases 5-fold: H4, H2B and H2A.Z are all acetylated at the cis-control elements but H3 remains unacetylated except at the -2.4 S silencer. Stimulation with LPS increases Lys expression a further 10-fold: this is accompanied by a rise in H3 acetylation throughout the cis-control elements; H4 and H2B acetylation remain substantial but acetylation at the Lys gene and its promoter remains low. Acetylation is thus concentrated at the cis-control elements, not at the Lys gene or its immediate promoter. H4 acetylation precedes H3 acetylation during development and H3 acetylation is most directly linked to high-level Lys expression.
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