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Molecular and Cellular Biology, September 2000, p. 6970-6983, Vol. 20, No. 18
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Conservation of Heterochromatin Protein 1 Function

Guozheng Wang,1,dagger Alicia Ma,1 Cheok-man Chow,2 David Horsley,1 Nicholas R. Brown,3 Ian G. Cowell,1,4 and Prim B. Singh1,4,*

Chromatin Function Laboratory, The Babraham Institute, Babraham, Cambridge CB2 4AT,1 Nuclear Reprogramming Laboratory, Division of Gene Expression and Development, Roslin Institute (Edinburgh), Midlothian, Scotland EH25 9PS,4 and Laboratory of Molecular Biophysics3 and Microbiology Unit,2 Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom

Received 24 January 2000/Returned for modification 27 March 2000/Accepted 12 June 2000

Heterochromatin represents a cytologically visible state of heritable gene repression. In the yeast, Schizosaccharomyces pombe, the swi6 gene encodes a heterochromatin protein 1 (HP1)-like chromodomain protein that localizes to heterochromatin domains, including the centromeres, telomeres, and the donor mating-type loci, and is involved in silencing at these loci. We identify here the functional domains of swi6p and demonstrate that the chromodomain from a mammalian HP1-like protein, M31, can functionally replace that of swi6p, showing that chromodomain function is conserved from yeasts to humans. Site-directed mutagenesis, based on a modeled three-dimensional structure of the swi6p chromodomain, shows that the hydrophobic amino acids which lie in the core of the structure are critical for biological function. Gel filtration, gel overlay experiments, and mass spectroscopy show that HP1 proteins can self-associate, and we suggest that it is as oligomers that HP1 proteins are incorporated into heterochromatin complexes that silence gene activity.

* Corresponding author. Mailing address: Nuclear Reprogramming Laboratory, Division of Gene Expression and Development, Roslin Institute (Edinburgh), Midlothian, Scotland, EH25 9PS, United Kingdom. Phone: 00-44-131-527-4239. Fax: 00-44-131-440-0434. E-mail: prim.singh{at}bbsrc.ac.uk.

dagger Present address: Molecular Medicine Group, School of Biological Sciences, University of Liverpool, Liverpool L69 72B, United Kingdom.

Molecular and Cellular Biology, September 2000, p. 6970-6983, Vol. 20, No. 18
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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