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MBC in Press, published online ahead of print February 21, 2007
Mol. Biol. Cell 10.1091/mbc.E06-01-0025

A more recent version of this article appeared on April 1, 2007
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Submitted on January 10, 2006
Revised on January 26, 2007
Accepted on February 5, 2007

Pericentromeric Heterochromatin Domains Are Maintained Without Accumulation of HP1

Julio Mateos-Langerak, Maartje C. Brink, Martijn S. Luijsterburg, Ineke van der Kraan, Roel van Driel, and Pernette J. Verschure

Swammerdam Institute for Life Sciences, BioCentrum Amsterdam, University of Amsterdam, 1098 SM Amsterdam, The Netherlands

Monitoring Editor: Wendy Bickmore

The heterochromatin protein 1 (HP1) family is thought to be an important structural component of heterochromatin. HP1 proteins bind via their chromodomain to nucleosomes methylated at lysine 9 of histone H3 (H3K9me). To investigate the role of HP1 in maintaining heterochromatin structure we used a dominant negative approach by expressing truncated HP1{alpha} or HP1{beta} proteins lacking a functional chromodomain. Expression of these truncated HP1 proteins individually or in combination resulted in a strong reduction of the accumulation of HP1{alpha}, HP1{beta} and HP1{gamma} in pericentromeric heterochromatin domains in mouse 3T3 fibroblasts. The expression levels of HP1 did not change. The apparent displacement of HP1{alpha}, HP1{beta} and HP1{gamma} from pericentromeric heterochromatin did not result in visible changes in the structure of pericentromeric heterochromatin domains, as visualized by DAPI staining and immunofluorescent labeling of H3K9me. Our results show that the accumulation of HP1{alpha}, HP1{beta} and HP1{gamma} at pericentromeric heterochromatin domains is not required to maintain DAPI stained pericentromeric heterochromatin domains and the methylated state of histone H3 at lysine 9 in such heterochromatin domains.

Address correspondence to: Pernette J. Verschure (pj.verschure{at}science.uva.nl)




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