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Ash1 counteracts Polycomb repression independent of histone H3 lysine 36 methylation
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
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2019 (English)In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 20, no 4, article id e46762Article in journal (Refereed) Published
Abstract [en]

Polycomb repression is critical for metazoan development. Equally important but less studied is the Trithorax system, which safeguards Polycomb target genes from the repression in cells where they have to remain active. It was proposed that the Trithorax system acts via methylation of histone H3 at lysine 4 and lysine 36 (H3K36), thereby inhibiting histone methyltransferase activity of the Polycomb complexes. Here we test this hypothesis by asking whether the Trithorax group protein Ash1 requires H3K36 methylation to counteract Polycomb repression. We show that Ash1 is the only Drosophila H3K36-specific methyltransferase necessary to prevent excessive Polycomb repression of homeotic genes. Unexpectedly, our experiments reveal no correlation between the extent of H3K36 methylation and the resistance to Polycomb repression. Furthermore, we find that complete substitution of the zygotic histone H3 with a variant in which lysine 36 is replaced by arginine does not cause excessive repression of homeotic genes. Our results suggest that the model, where the Trithorax group proteins methylate histone H3 to inhibit the histone methyltransferase activity of the Polycomb complexes, needs revision.

Place, publisher, year, edition, pages
WILEY , 2019. Vol. 20, no 4, article id e46762
Keywords [en]
Ash1, Drosophila, Polycomb, Trithorax
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-158742DOI: 10.15252/embr.201846762ISI: 000463235300017PubMedID: 30833342OAI: oai:DiVA.org:umu-158742DiVA, id: diva2:1316656
Available from: 2019-05-20 Created: 2019-05-20 Last updated: 2019-05-20Bibliographically approved

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Dorafshan, EshaghKahn, Tatyana G.Glotov, AlexanderSavitsky, MikhailSchwartz, Yuri B.

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Dorafshan, EshaghKahn, Tatyana G.Glotov, AlexanderSavitsky, MikhailSchwartz, Yuri B.
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