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  Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

Kalb, R., Latwiel, S., Baymaz, H. I., Jansen, P. W. T. C., Müller, C. W., Vermeulen, M., et al. (2014). Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 21(6), 569-571. doi:10.1038/nsmb.2833.

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 Creators:
Kalb, Reinhard1, Author           
Latwiel, Sebastian2, Author
Baymaz, H. Irem2, Author
Jansen, Pascal W. T. C.2, Author
Müller, Christoph W.2, Author
Vermeulen, Michiel2, Author
Müller, Jürg1, Author           
Affiliations:
1Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565161              
2external, ou_persistent22              

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Free keywords: PRC2; COMPLEX; METHYLTRANSFERASES; UBIQUITINATION; EXPRESSION; CHROMATIN; TARGETS; JARID2
 Abstract: A key step in gene repression by Polycomb is trimethylation of histone H3 K27 by PCR2 to form H3K27me3. H3K27me3 provides a binding surface for PRC1. We show that monoubiquitination of histone H2A by PRC1-type complexes to form H2Aub creates a binding site for Jarid2-Aebp2 containing PRC2 and promotes H3K27 trimethylation on H2Aub nucleosomes. Jarid2, Aebp2 and H2Aub thus constitute components of a positive feedback loop establishing H3K27me3 chromatin domains.

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Language(s): eng - English
 Dates: 2014-06
 Publication Status: Issued
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000337010500012
DOI: 10.1038/nsmb.2833
 Degree: -

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Title: NATURE STRUCTURAL & MOLECULAR BIOLOGY
Source Genre: Journal
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Publ. Info: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 21 (6) Sequence Number: - Start / End Page: 569 - 571 Identifier: ISSN: 1545-9993