Published online 2 February 2004
Nucleic Acids Research, 2004, Vol. 32, No. 2 736-741
© 2004 Oxford University Press
Fission yeast Arp6 is required for telomere silencing, but functions independently of Swi6
Department of Chemistry and 1 Department of Biology, Shizuoka University, 836 Oya, Shizuoka 422-8529, Japan, 2 Department of Viral Oncology, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan and 3 Department of Molecular and Cell Biology, Tohoku University, Aoba-ku, Sendai 981-8555, Japan
*To whom correspondence should be addressed. Tel: +81 54 238 4762; Fax: +81 54 237 3384; Email: scmueno{at}ipc.shizuoka.ac.jp
The actin-related proteins (Arps), which are subdivided into at least eight subfamilies, are conserved from yeast to humans. A member of the Arp6 subfamily in Drosophila, Arp4/Arp6, co-localizes with heterochromatin protein 1 (HP1) in pericentric heterochromatin. Fission yeast Schizosaccharomyces pombe possesses both an HP1 homolog and an Arp6 homolog. However, the function of S.pombe Arp6 has not been characterized yet. We found that deletion of arp6+ impaired telomere silencing, but did not affect centromere silencing. Chromatin immunoprecipitation assays revealed that Arp6 bound to the telomere region. However, unlike Drosophila Arp4/Arp6, S.pombe Arp6 was distributed throughout nuclei. The binding of Arp6 to telomere DNA was not affected by deletion of swi6+. Moreover, the binding of Swi6 to telomere ends was not affected by deletion of arp6+. These results suggest that Arp6 and Swi6 function independently at telomere ends. We propose that the Arp6-mediated repression mechanism works side by side with Swi6-based telomere silencing in S.pombe.
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