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Drosophila dSet2 functions in H3-K36 methylation and is required for development.
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Science and Technology).
2007 (English)In: Biochem Biophys Res Commun, ISSN 0006-291X, Vol. 359, no 3, 784-9 p.Article in journal (Refereed) Published
Abstract [en]

Lysine methylation has important functions in biological processes that range from heterochromatin formation to transcription regulation. Here, we demonstrate that Drosophila dSet2 encodes a developmentally essential histone H3 lysine 36 (K36) methyltransferase. Larvae subjected to RNA interference-mediated (RNAi) suppression of dSet2 lack dSet2 expression and H3-K36 methylation, indicating that dSet2 is the sole enzyme responsible for this modification in Drosophila melanogaster. dSet2 RNAi blocks puparium formation and adult development, and causes partial (blister) separation of the dorsal and ventral wing epithelia, defects suggesting a failure of the ecdysone-controlled genetic program. A transheterozygous EcR null mutation/dSet2 RNAi combination produces a complete (balloon) separation of the wing surfaces, revealing a genetic interaction between EcR and dSet2. Using immunoprecipitation, we demonstrate that dSet2 associates with the hyperphosphorylated form of RNA polymerase II (RNAPII).

Place, publisher, year, edition, pages
2007. Vol. 359, no 3, 784-9 p.
Keyword [en]
Animals, Drosophila Proteins/genetics/*metabolism, Drosophila melanogaster/genetics/*growth & development/*metabolism, Gene Expression Regulation; Developmental, Histone-Lysine N-Methyltransferase/genetics/*metabolism, Histones/*metabolism, Lysine/genetics/*metabolism, Methylation, Phosphorylation, Protein Binding, RNA Polymerase II/metabolism, Receptors; Steroid/genetics/metabolism
Identifiers
URN: urn:nbn:se:umu:diva-17028PubMedID: 17560546OAI: oai:DiVA.org:umu-17028DiVA: diva2:156701
Available from: 2008-01-12 Created: 2008-01-12 Last updated: 2011-01-11Bibliographically approved

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Larsson, Jan
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CiteExportLink to record
Permanent link

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Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
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  • nn-NO
  • nn-NB
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More languages
Output format
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