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  H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming

Daujat, S., Weiss, T., Mohn, F., Lange, U. C., Ziegler-Birling, C., Zeissler, U., et al. (2009). H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming. Nature Structural & Molecular Biology, 16(7), 777-781. doi:10.1038/nsmb.1629.

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Genre: Zeitschriftenartikel
Alternativer Titel : Nature Struct & Mol Biol

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Daujat, Sylvain, Autor
Weiss, Thomas, Autor
Mohn, Fabio, Autor
Lange, Ulrike C., Autor
Ziegler-Birling, Céline, Autor
Zeissler, Ulrike, Autor
Lappe, Michael1, Autor           
Schübeler, Dirk, Autor
Torres-Padilla, Maria-Elena, Autor
Schneider, Robert, Autor
Affiliations:
1Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433554              

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 Zusammenfassung: Histone modifications are central to the regulation of all DNA-dependent processes. Lys64 of histone H3 (H3K64) lies within the globular domain at a structurally important position. We identify trimethylation of H3K64 (H3K64me3) as a modification that is enriched at pericentric heterochromatin and associated with repeat sequences and transcriptionally inactive genomic regions. We show that this new mark is dynamic during the two main epigenetic reprogramming events in mammals. In primordial germ cells, H3K64me3 is present at the time of specification, but it disappears transiently during reprogramming. In early mouse embryos, it is inherited exclusively maternally; subsequently, the modification is rapidly removed, suggesting an important role for H3K64me3 turnover in development. Taken together, our findings establish H3K64me3 as a previously uncharacterized histone modification that is preferentially localized to repressive chromatin. We hypothesize that H3K64me3 helps to 'secure' nucleosomes, and perhaps the surrounding chromatin, in an appropriately repressed state during development.

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Sprache(n): eng - English
 Datum: 2009-07
 Publikationsstatus: Erschienen
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Titel: Nature Structural & Molecular Biology
  Alternativer Titel : Nature Struct & Mol Biol
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 16 (7) Artikelnummer: - Start- / Endseite: 777 - 781 Identifikator: ISSN: 1545-9993