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  Regulation and function of H3K36 di-methylation by the trithorax-group protein complex AMC

Schmähling, S., Meiler, A., Lee, Y., Mohammed, A., Finkl, K., Tauscher, K., et al. (2018). Regulation and function of H3K36 di-methylation by the trithorax-group protein complex AMC. Development, 145(7): UNSP dev163808. doi:10.1242/dev.163808.

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© 2018. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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 Creators:
Schmähling, Sigrun1, Author              
Meiler, Arno2, Author              
Lee, Yoonjung3, Author
Mohammed, Arif1, Author              
Finkl, Katja1, Author              
Tauscher, Katharina1, Author              
Israel, Lars3, Author
Wirth, Marc3, Author
Philippou-Massier, Julia3, Author
Blum, Helmut3, Author
Habermann, Bianca4, Author              
Imhof, Axel3, Author
Song, Ji-Joon3, Author
Müller, Jürg1, Author              
Affiliations:
1Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565161              
2Pichlmair, Andreas / Innate Immunity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565166              
3external, ou_persistent22              
4Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1832284              

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Free keywords: POLYCOMB GROUP PROTEINS; RNA-POLYMERASE-II; HISTONE H3; STRUCTURAL BASIS; TRANSCRIPTIONAL ELONGATION; SACCHAROMYCES-CEREVISIAE; DROSOPHILA-MELANOGASTER; GENE-EXPRESSION; CHROMO DOMAIN; MRG DOMAINSDevelopmental Biology; Trithorax group; Ash1; MRG15; Histone H3K36 methylation; Drosophila;
 Abstract: The Drosophila Ash1 protein is a trithorax-group (trxG) regulator that antagonizes Polycomb repression at HOX genes. Ash1 di-methylates lysine 36 in histone H3 (H3K36me2) but how this activity is controlled and at which genes it functions is not well understood. We show that Ash1 protein purified from Drosophila exists in a complex with MRG15 and Caf1 that we named AMC. In Drosophila and human AMC, MRG15 binds a conserved FxLP motif near the Ash1 SET domain and stimulates H3K36 di-methylation on nucleosomes. Drosophila MRG15-null and ash1 catalytic mutants show remarkably specific trxG phenotypes: stochastic loss of HOX gene expression and homeotic transformations in adults. In mutants lacking AMC, H3K36me2 bulk levels appear undiminished but H3K36me2 is reduced in the chromatin of HOX and other AMC-regulated genes. AMC therefore appears to act on top of the H3K36me2/me3 landscape generated by the major H3K36 methyltransferases NSD and Set2. Our analyses suggest that H3K36 di-methylation at HOX genes is the crucial physiological function of AMC and the mechanism by which the complex antagonizes Polycomb repression at these genes.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000438944000009
DOI: 10.1242/dev.163808
 Degree: -

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Title: Development
  Other : Development
Source Genre: Journal
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Publ. Info: Cambridge, Cambridgeshire : Company of Biologists
Pages: - Volume / Issue: 145 (7) Sequence Number: UNSP dev163808 Start / End Page: - Identifier: ISSN: 0950-1991
CoNE: https://pure.mpg.de/cone/journals/resource/954927546241