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Vol. 16, No. 14, pp. 1766-1778, July 15, 2002
1 Institute for Virus Research, Kyoto University, Kyoto
606-8507, Japan; 2 Graduate program in Molecular Biology,
Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA;
3 Medical Research Center Human Genetics Unit, Western General
Hospital, Edinburgh EH4 2XU, Scotland, UK; 4 Cold Spring
Harbor Laboratory, Cold Spring Harbor, New York 11724, USA;
5 Faculty of Life and Environmental Science, Shimane
University, Matsue 690-8504, Japan
Heterochromatin is a functionally important chromosomal component,
especially at centromeres. In fission yeast, conserved heterochromatin-specific modifications of the histone H3 tail, involving deacetylation of Lys 9 and Lys 14 and subsequent methylation of Lys 9, promote the recruitment of a heterochromatin protein, Swi6, a
homolog of the Drosophila heterochromatin protein 1. However, the primary determinants of the positioning of heterochromatin are
still unclear. The fission yeast proteins Abp1, Cbh1, and Cbh2 are
homologs of the human protein CENP-B that bind to centromeric 
-satellite DNA and associate with centromeric heterochromatin. We
show that the CENP-B homologs are functionally redundant at centromeres, and that Abp1 binds specifically to centromeric
heterochromatin. In the absence of Abp1 or Cbh1, the centromeric
association of Swi6 is diminished, resulting in a decrease in silencing
of the region. CENP-B-homolog double disruptants show a synergistic
reduction of Swi6 at centromeric heterochromatin, indicating that the
three proteins are functionally redundant in the recruitment of Swi6. Furthermore, using chromatin immunoprecipitation assays, we show that
disruption of CENP-B homologs causes a decrease in
heterochromatin-specific modifications of histone H3. These results
indicate that the CENP-B homologs act as site-specific nucleation
factors for the formation of centromeric heterochromatin by
heterochromatin-specific modifications of histone tails.
[Key Words: CENP-B; heterochromatin; centromere; histone modification; fission yeast]
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