H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming

Standard

H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming. / Daujat, Sylvain; Weiss, Thomas; Mohn, Fabio; Lange, Ulrike C; Ziegler-Birling, Céline; Zeissler, Ulrike; Lappe, Michael; Schübeler, Dirk; Torres-Padilla, Maria-Elena; Schneider, Robert.

in: NAT STRUCT MOL BIOL, Jahrgang 16, Nr. 7, 01.07.2009, S. 777-81.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Daujat, S, Weiss, T, Mohn, F, Lange, UC, Ziegler-Birling, C, Zeissler, U, Lappe, M, Schübeler, D, Torres-Padilla, M-E & Schneider, R 2009, 'H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming', NAT STRUCT MOL BIOL, Jg. 16, Nr. 7, S. 777-81. https://doi.org/10.1038/nsmb.1629

APA

Daujat, S., Weiss, T., Mohn, F., Lange, U. C., Ziegler-Birling, C., Zeissler, U., Lappe, M., Schübeler, D., Torres-Padilla, M-E., & Schneider, R. (2009). H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming. NAT STRUCT MOL BIOL, 16(7), 777-81. https://doi.org/10.1038/nsmb.1629

Vancouver

Bibtex

@article{f2a8ef716f1d4f9983442cd9aaab9113,
title = "H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming",
abstract = "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.",
keywords = "Histone , Cell Line, chromatin, DNA Methylation, Embryo, Mammalian, Epigenetics, Heterochromatin, Histones, Lysine, Methyltransferases, Mice, Molecular Sequence Data, Protein Conformation",
author = "Sylvain Daujat and Thomas Weiss and Fabio Mohn and Lange, {Ulrike C} and C{\'e}line Ziegler-Birling and Ulrike Zeissler and Michael Lappe and Dirk Sch{\"u}beler and Maria-Elena Torres-Padilla and Robert Schneider",
year = "2009",
month = jul,
day = "1",
doi = "10.1038/nsmb.1629",
language = "English",
volume = "16",
pages = "777--81",
journal = "NAT STRUCT MOL BIOL",
issn = "1545-9993",
publisher = "NATURE PUBLISHING GROUP",
number = "7",

}

RIS

TY - JOUR

T1 - H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming

AU - Daujat, Sylvain

AU - Weiss, Thomas

AU - Mohn, Fabio

AU - Lange, Ulrike C

AU - Ziegler-Birling, Céline

AU - Zeissler, Ulrike

AU - Lappe, Michael

AU - Schübeler, Dirk

AU - Torres-Padilla, Maria-Elena

AU - Schneider, Robert

PY - 2009/7/1

Y1 - 2009/7/1

N2 - 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.

AB - 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.

KW - Histone

KW - Cell Line

KW - chromatin

KW - DNA Methylation

KW - Embryo, Mammalian

KW - Epigenetics

KW - Heterochromatin

KW - Histones

KW - Lysine

KW - Methyltransferases

KW - Mice

KW - Molecular Sequence Data

KW - Protein Conformation

U2 - 10.1038/nsmb.1629

DO - 10.1038/nsmb.1629

M3 - SCORING: Journal article

C2 - 19561610

VL - 16

SP - 777

EP - 781

JO - NAT STRUCT MOL BIOL

JF - NAT STRUCT MOL BIOL

SN - 1545-9993

IS - 7

ER -