Nucleic Acids Research Advance Access originally published online on October 4, 2006
Nucleic Acids Research 2006 34(19):5461-5470; doi:10.1093/nar/gkl687
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Nucleic Acids Research, 2006, Vol. 34, No. 19 5461-5470
© 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 Arabidopsis SUVR4 protein is a nucleolar histone methyltransferase with preference for monomethylated H3K9
Department of Molecular Biosciences, University of Oslo P.O. Box 1041 Blindern, N-0316 Oslo, Norway 1 Institute of Genetics, Biologicum, Martin Luther University Halle Halle, Germany
*To whom correspondence should be addressed. Tel: +47 22857297; Fax: +47 22856041; Email: reidunn.aalen{at}imbv.uio.no
Received May 5, 2006. Revised September 4, 2006. Accepted September 7, 2006.
Proteins containing the evolutionarily conserved SET domain are involved in regulation of eukaryotic gene expression and chromatin structure through their histone lysine methyltransferase (HMTase) activity. The Drosophila SU(VAR)3-9 protein and related proteins of other organisms have been associated with gene repression and heterochromatinization. In Arabidopsis there are 10 SUVH and 5 SUVR genes encoding proteins similar to SU(VAR)3-9, and 4 SUVH proteins have been shown to control heterochromatic silencing by its HMTase activity and by directing DNA methylation. The SUVR proteins differ from the SUVH proteins in their domain structure, and we show that the closely related SUVR1, SUVR2 and SUVR4 proteins contain a novel domain at their N-terminus, and a SUVR specific region preceding the SET domain. Green fluorescent protein (GFP)-fusions of these SUVR proteins preferably localize to the nucleolus, suggesting involvement in regulation of rRNA expression, in contrast to other SET-domain proteins studied so far. A novel HMTase specificity was demonstrated for SUVR4, in that monomethylated histone H3K9 is its preferred substrate in vitro.
Present address: Sylvia S. Johnsen, Institute of Medical Biology, University of Tromsø, 9037 Tromsø, Norway
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