Epigenetic aspects of HP1 exchange kinetics in apoptotic chromatin
Language English Country France Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
23023195
DOI
10.1016/j.biochi.2012.09.027
PII: S0300-9084(12)00387-2
Knihovny.cz E-resources
- MeSH
- Acetylation MeSH
- Apoptosis drug effects MeSH
- Cell Adhesion MeSH
- Chromatin drug effects genetics metabolism MeSH
- Chromosomal Proteins, Non-Histone genetics metabolism MeSH
- Epigenesis, Genetic drug effects MeSH
- Etoposide MeSH
- Fibroblasts cytology drug effects metabolism MeSH
- Antineoplastic Agents, Phytogenic MeSH
- Histones genetics metabolism MeSH
- Chromobox Protein Homolog 5 MeSH
- Kinetics MeSH
- Humans MeSH
- Methylation MeSH
- Mice MeSH
- Cell Line, Tumor MeSH
- Tumor Suppressor Protein p53 genetics metabolism MeSH
- Protein Processing, Post-Translational drug effects MeSH
- Proto-Oncogene Proteins c-bcl-2 genetics metabolism MeSH
- Recombinant Fusion Proteins genetics metabolism MeSH
- Signal Transduction drug effects MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- CBX1 protein, human MeSH Browser
- Cbx1 protein, mouse MeSH Browser
- CBX5 protein, human MeSH Browser
- Chromatin MeSH
- Chromosomal Proteins, Non-Histone MeSH
- Etoposide MeSH
- Antineoplastic Agents, Phytogenic MeSH
- Histones MeSH
- Chromobox Protein Homolog 5 MeSH
- Tumor Suppressor Protein p53 MeSH
- Proto-Oncogene Proteins c-bcl-2 MeSH
- Recombinant Fusion Proteins MeSH
Apoptotic bodies are the most condensed form of chromatin. In general, chromatin structure and function are mostly dictated by histone post-translational modifications. Thus, we have analyzed the histone signature in apoptotic cells, characterized by pronounced chromatin condensation. Here, H2B mono-acetylation, and H3K9 and H4 acetylation was significantly decreased in apoptotic cells, which maintained a high level of H3K9 methylation. This phenotype was independent of p53 function and distinct levels of anti-apoptotic Bcl2 protein. Interestingly, after etoposide treatment of leukemia and multiple myeloma cells, H3K9 and H4 hypoacetylation was accompanied by increased H3K9me2, but not H3K9me1 or H3K9me3. In adherent mouse fibroblasts, a high level of H3K9me3 and histone deacetylation in apoptotic bodies was likely responsible for the pronounced (∼40%) recovery of GFP-HP1α and GFP-HP1β after photobleaching. HP1 mobility in apoptotic cells appeared to be unique because limited exchange after photobleaching was observed for other epigenetically important proteins, including GFP-JMJD2b histone demethylase (∼10% fluorescence recovery) or Polycomb group-related GFP-BMI1 protein (∼20% fluorescence recovery). These findings imply a novel fact that only certain subset of proteins in apoptotic bodies is dynamic.
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