Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin

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Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin. / Lange, Ulrike C; Siebert, Stéphanie; Wossidlo, Mark; Weiss, Thomas; Ziegler-Birling, Céline; Walter, Jörn; Torres-Padilla, Maria-Elena; Daujat, Sylvain; Schneider, Robert.

In: NAT COMMUN, Vol. 4, 01.01.2013, p. 2233.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Lange, UC, Siebert, S, Wossidlo, M, Weiss, T, Ziegler-Birling, C, Walter, J, Torres-Padilla, M-E, Daujat, S & Schneider, R 2013, 'Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin', NAT COMMUN, vol. 4, pp. 2233. https://doi.org/10.1038/ncomms3233

APA

Lange, U. C., Siebert, S., Wossidlo, M., Weiss, T., Ziegler-Birling, C., Walter, J., Torres-Padilla, M-E., Daujat, S., & Schneider, R. (2013). Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin. NAT COMMUN, 4, 2233. https://doi.org/10.1038/ncomms3233

Vancouver

Lange UC, Siebert S, Wossidlo M, Weiss T, Ziegler-Birling C, Walter J et al. Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin. NAT COMMUN. 2013 Jan 1;4:2233. https://doi.org/10.1038/ncomms3233

Bibtex

@article{c2842899c96e4aab8931798109bfe603,
title = "Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin",
abstract = "To ensure genome stability, pericentromeric regions are compacted in a dense heterochromatic structure through a combination of specific 'epigenetic' factors and modifications. A cascadal pathway is responsible for establishing pericentromeric chromatin involving chromatin modifiers and 'readers', such as H3K9 histone methyltransferases (Suv)39h and heterochromatin protein 1. Here we define how H3K64me3 on the lateral surface of the histone octamer integrates within the heterochromatinization cascade. Our data suggest that enrichment of H3K64me3 at pericentromeric chromatin foci is dependent on H3K9me3 but independent of a number of central factors such as heterochromatin protein 1, DNA methyltransferases and Suv4-20h histone methyltransferases. Our results support a model in which pericentromeric heterochromatin foci are formed along distinct pathways upon H3K9 trimethylation, involving H3K64me3 to potentially stabilize DNA-histone interactions, as well as sequential recruitment of repressive histone tail and DNA modifications. We hence suggest that multiple mechanisms ensure heterochromatin integrity at pericentromeres, with H3K64me3 as an important factor.",
keywords = "centromere, Histone, Chromatin, Lysine methylation, Heterochromatin",
author = "Lange, {Ulrike C} and St{\'e}phanie Siebert and Mark Wossidlo and Thomas Weiss and C{\'e}line Ziegler-Birling and J{\"o}rn Walter and Maria-Elena Torres-Padilla and Sylvain Daujat and Robert Schneider",
year = "2013",
month = jan,
day = "1",
doi = "10.1038/ncomms3233",
language = "English",
volume = "4",
pages = "2233",
journal = "NAT COMMUN",
issn = "2041-1723",
publisher = "NATURE PUBLISHING GROUP",

}

RIS

TY - JOUR

T1 - Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin

AU - Lange, Ulrike C

AU - Siebert, Stéphanie

AU - Wossidlo, Mark

AU - Weiss, Thomas

AU - Ziegler-Birling, Céline

AU - Walter, Jörn

AU - Torres-Padilla, Maria-Elena

AU - Daujat, Sylvain

AU - Schneider, Robert

PY - 2013/1/1

Y1 - 2013/1/1

N2 - To ensure genome stability, pericentromeric regions are compacted in a dense heterochromatic structure through a combination of specific 'epigenetic' factors and modifications. A cascadal pathway is responsible for establishing pericentromeric chromatin involving chromatin modifiers and 'readers', such as H3K9 histone methyltransferases (Suv)39h and heterochromatin protein 1. Here we define how H3K64me3 on the lateral surface of the histone octamer integrates within the heterochromatinization cascade. Our data suggest that enrichment of H3K64me3 at pericentromeric chromatin foci is dependent on H3K9me3 but independent of a number of central factors such as heterochromatin protein 1, DNA methyltransferases and Suv4-20h histone methyltransferases. Our results support a model in which pericentromeric heterochromatin foci are formed along distinct pathways upon H3K9 trimethylation, involving H3K64me3 to potentially stabilize DNA-histone interactions, as well as sequential recruitment of repressive histone tail and DNA modifications. We hence suggest that multiple mechanisms ensure heterochromatin integrity at pericentromeres, with H3K64me3 as an important factor.

AB - To ensure genome stability, pericentromeric regions are compacted in a dense heterochromatic structure through a combination of specific 'epigenetic' factors and modifications. A cascadal pathway is responsible for establishing pericentromeric chromatin involving chromatin modifiers and 'readers', such as H3K9 histone methyltransferases (Suv)39h and heterochromatin protein 1. Here we define how H3K64me3 on the lateral surface of the histone octamer integrates within the heterochromatinization cascade. Our data suggest that enrichment of H3K64me3 at pericentromeric chromatin foci is dependent on H3K9me3 but independent of a number of central factors such as heterochromatin protein 1, DNA methyltransferases and Suv4-20h histone methyltransferases. Our results support a model in which pericentromeric heterochromatin foci are formed along distinct pathways upon H3K9 trimethylation, involving H3K64me3 to potentially stabilize DNA-histone interactions, as well as sequential recruitment of repressive histone tail and DNA modifications. We hence suggest that multiple mechanisms ensure heterochromatin integrity at pericentromeres, with H3K64me3 as an important factor.

KW - centromere

KW - Histone

KW - Chromatin

KW - Lysine methylation

KW - Heterochromatin

U2 - 10.1038/ncomms3233

DO - 10.1038/ncomms3233

M3 - SCORING: Journal article

C2 - 23903902

VL - 4

SP - 2233

JO - NAT COMMUN

JF - NAT COMMUN

SN - 2041-1723

ER -