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Molecular and Cellular Biology, August 2002, p. 5539-5553, Vol. 22, No. 15
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.15.5539-5553.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Selective Interactions between Vertebrate Polycomb Homologs and the SUV39H1 Histone Lysine Methyltransferase Suggest that Histone H3-K9 Methylation Contributes to Chromosomal Targeting of Polycomb Group Proteins

Richard G. A. B. Sewalt,1 Monika Lachner,2 Mark Vargas,1 Karien M. Hamer,1 Jan L. den Blaauwen,1 Thijs Hendrix,1 Martin Melcher,2,{dagger} Dieter Schweizer,3 Thomas Jenuwein,2 and Arie P. Otte1*

Swammerdam Institute for Life Sciences, BioCentrum Amsterdam, University of Amsterdam, 1018 TV Amsterdam, The Netherlands,1 Research Institute of Molecular Pathology, The Vienna Biocenter,2 Institute of Botany, University of Vienna, A-1030 Vienna, Austria3

Received 14 March 2002/ Accepted 25 April 2002

Polycomb group (PcG) proteins form multimeric chromatin-associated protein complexes that are involved in heritable repression of gene activity. Two distinct human PcG complexes have been characterized. The EED/EZH2 PcG complex utilizes histone deacetylation to repress gene activity. The HPC/HPH PcG complex contains the HPH, RING1, BMI1, and HPC proteins. Here we show that vertebrate Polycomb homologs HPC2 and XPc2, but not M33/MPc1, interact with the histone lysine methyltransferase (HMTase) SUV39H1 both in vitro and in vivo. We further find that overexpression of SUV39H1 induces selective nuclear relocalization of HPC/HPH PcG proteins but not of the EED/EZH2 PcG proteins. This SUV39H1-dependent relocalization concentrates the HPC/HPH PcG proteins to the large pericentromeric heterochromatin domains (1q12) on human chromosome 1. Within these PcG domains we observe increased H3-K9 methylation. Finally, we show that H3-K9 HMTase activity is associated with endogenous HPC2. Our findings suggest a role for the SUV39H1 HMTase and histone H3-K9 methylation in the targeting of human HPC/HPH PcG proteins to modified chromatin structures.

* Corresponding author. Mailing address: Swammerdam Institute for Life Sciences, BioCentrum Amsterdam, University of Amsterdam, Plantage Muidergracht 12, 1018 TV Amsterdam, The Netherlands. Phone: 31-20-5255115. Fax: 31-20-5255090. E-mail: arie.otte{at}science.uva.nl.

{dagger} Present address: Institute of Immunology, University of Vienna, A-1235 Vienna, Austria.

Molecular and Cellular Biology, August 2002, p. 5539-5553, Vol. 22, No. 15
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.15.5539-5553.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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