Histone H4 lysine 12 acetylation regulates telomeric heterochromatin plasticity in Saccharomyces cerevisiae
| Autor: | Brian A. Lenzmeier, Xiao-Hong Fu, Jin-Qiu Zhou, Wei Dang, Shanshan Wang, Bo O. Zhou, Yang Zhang |
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| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
DNA Replication
Cancer Research Saccharomyces cerevisiae Proteins Transcription Genetic Histone acetyltransferase complex lcsh:QH426-470 Heterochromatin Telomeric heterochromatin Saccharomyces cerevisiae Biology Molecular Biology/Histone Modification Histones Histone H4 Genetics Molecular Biology/Chromatin Structure Telomerase Molecular Biology Genetics (clinical) Ecology Evolution Behavior and Systematics Histone Acetyltransferases Recombination Genetic Lysine EZH2 SIR proteins Acetylation Telomere Molecular biology Cell biology lcsh:Genetics Histone biology.protein Heterochromatin protein 1 Research Article |
| Zdroj: | PLoS Genetics, Vol 7, Iss 1, p e1001272 (2011) PLoS Genetics |
| ISSN: | 1553-7404 1553-7390 |
| Popis: | Recent studies have established that the highly condensed and transcriptionally silent heterochromatic domains in budding yeast are virtually dynamic structures. The underlying mechanisms for heterochromatin dynamics, however, remain obscure. In this study, we show that histones are dynamically acetylated on H4K12 at telomeric heterochromatin, and this acetylation regulates several of the dynamic telomere properties. Using a de novo heterochromatin formation assay, we surprisingly found that acetylated H4K12 survived the formation of telomeric heterochromatin. Consistently, the histone acetyltransferase complex NuA4 bound to silenced telomeric regions and acetylated H4K12. H4K12 acetylation prevented the over-accumulation of Sir proteins at telomeric heterochromatin and elimination of this acetylation caused defects in multiple telomere-related processes, including transcription, telomere replication, and recombination. Together, these data shed light on a potential histone acetylation mark within telomeric heterochromatin that contributes to telomere plasticity. Author Summary The genetic material in eukaryotes is packaged into chromatin. The chromatin structure is orchestrated such that euchromatic regions are relatively uncondensed and accessible to factors that bind DNA, whereas heterochromatic regions are densely packaged into higher-order conformations. The compact nature for heterochromatin may endanger normal DNA metabolism, such as DNA replication and recombination. We found that targeted histone acetylation provided a way for cells to maintain a relatively plastic heterochromatin structure that is necessary for DNA metabolisms within telomeric heterochromatin. Therefore, although heterochromatic domains are largely silenced, they are not as static as we previously assumed, and the dynamic aspect of heterochromatin is directly attributable to changes in its own chemical properties. |
| Databáze: | OpenAIRE |
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