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Nucleic Acids Research Advance Access originally published online on September 8, 2006
Nucleic Acids Research 2006 34(16):4609-4621; doi:10.1093/nar/gkl640
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Nucleic Acids Research, 2006, Vol. 34, No. 16 4609-4621
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (
http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.


Molecular Biology

The Drosophila G9a gene encodes a multi-catalytic histone methyltransferase required for normal development

Marianne Stabell, Ragnhild Eskeland1, Mona Bjørkmo, Jan Larsson2, Reidunn B. Aalen, Axel Imhof1 and Andrew Lambertsson*

Department of Molecular Biosciences, University of Oslo PO Box 1041, Blindern, NO-0316 Oslo, Norway 1 Adolf-Butenandt Institute, Department of Molecular Biology, Histone Modifications Group and Protein Analysis Unit, Ludwig-Maximillians University of Munich Schillerstrasse 44, DE-80336 Munich, Germany 2 UCMP, Umeå University SE-901 87 Umeå, Sweden

*To whom correspondence should be addressed. Tel: +47 22 85 48 94; Fax: +47 22 85 47 26; Email: g.a.lambertsson{at}imbv.uio.no

Received June 6, 2006. Revised July 24, 2006. Accepted August 17, 2006.

Mammalian G9a is a histone H3 Lys-9 (H3–K9) methyltransferase localized in euchromatin and acts as a co-regulator for specific transcription factors. G9a is required for proper development in mammals as g9a/g9a mice show growth retardation and early lethality. Here we describe the cloning, the biochemical and genetical analyses of the Drosophila homolog dG9a. We show that dG9a shares the structural organization of mammalian G9a, and that it is a multi-catalytic histone methyltransferase with specificity not only for lysines 9 and 27 on H3 but also for H4. Surprisingly, it is not the H4–K20 residue that is the target for this methylation. Spatiotemporal expression analyses reveal that dG9a is abundantly expressed in the gonads of both sexes, with no detectable expression in gonadectomized adults. In addition we find a low but clearly observable level of dG9a transcript in developing embryos, larvae and pupae. Genetic and RNAi experiments reveal that dG9a is involved in ecdysone regulatory pathways.


Present address: Mona Bjørkmo, The Biotechnology Centre of Oslo, University of Oslo, NO-0317 Oslo, Norway


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