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Molecular and Cellular Biology, September 2000, p. 6970-6983, Vol. 20, No. 18
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.
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Conservation of Heterochromatin Protein 1 Function

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