Published online 14 June 2004. doi:10.1083/jcb.200312061
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 6, 759-765
The fission yeast heterochromatin protein Rik1 is required for telomere clustering during meiosis
Creighton T. Tuzon1,2,
Britta Borgstrom3,
Dietmar Weilguny3,
Richard Egel3,
Julia Promisel Cooper1,2, and
Olaf Nielsen3
1 Telomere Biology Laboratory, Cancer Research UK, London WC2A 3PX, England, UK
2 Department of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, CO 80262
3 Institute of Molecular Biology, University of Copenhagen, DK-1353 Copenhagen K, Denmark
Address correspondence to Olaf Nielsen, Department of Genetics, Institute of Molecular Biology, University of Copenhagen, Oster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark. Tel.: 45 3532 2102. Fax: 45 3532 2113. email: onigen{at}biobase.dk; or Julia Promisel Cooper, Telomere Biology Laboratory, Cancer Research UK, 44 Lincoln's Inn Fields, London WC2A 3PX, UK. Tel.: 44 207 269 3415. Fax: 44 207 269 3258. email: julie.cooper{at}cancer.org.uk
Abstract
Telomeres share the ability to silence nearby transcription with heterochromatin, but the requirement of heterochromatin proteins for most telomere functions is unknown. The fission yeast Rik1 protein is required for heterochromatin formation at centromeres and the mating-type locus, as it recruits the Clr4 histone methyltransferase, whose modification of histone H3 triggers binding by Swi6, a conserved protein involved in spreading of heterochromatin. Here, we demonstrate that Rik1 and Clr4, but not Swi6, are required along with the telomere protein Taz1 for crucial chromosome movements during meiosis. However, Rik1 is dispensable for the protective roles of telomeres in preventing chromosome end-fusion. Thus, a Swi6-independent heterochromatin function distinct from that at centromeres and the mating-type locus operates at telomeres during sexual differentiation.
Key Words: horsetail movement; histone methylation; chromosome behavior; silencing; S. pombe
D. Weilguny's present address is NatImmune A/S, Fruebjergvej 3, DK-2100 Copenhagen O, Denmark.
Abbreviations used in this paper: NHEJ, nonhomologous end-joining; SPB, spindle pole body.

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