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Letters to Nature
Nature 385, 744 - 747 (20 February 1997); doi:10.1038/385744a0

Regulation of telomere length and function by a Myb-domain protein in fission yeast

Julia Promisel Cooper*, Elaine R. Nimmo, Robin C. Allshire & Thomas R. Cech*

*Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309, USA
MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK
Present address: Imperial Cancer Research Fund, Lincoln's Inn Fields, London WC2A 3PX, UK

Telomeres, the specialized nucleoprotein structures that comprise the ends of eukaryotic chromosomes1,2, are essential for complete replication3–5, and regulation of their length has been a focus of research on tumorigenesis6–8. In the budding yeast Saccharomyces cerevisiae, the protein Raplp binds to telomeric DNA and functions in the regulation of telomere length9–12. A human telomere protein, hTRF (human TTAGGG repeat factor) binds the telomere sequence in vitro 13 and localizes to telomeres cytologically14, but its functions are not yet known. Here we use a genetic screen to identify a telomere protein in fission yeast, Tazlp (telomere-associated in Schizosaccharomyces pombe), that shares homology to the Myb proto-oncogene DNA-binding domain with hTRF. Disruption or deletion of the taz1 + gene causes a massive increase in telomere length. Tazlp is required for the repression of telomere-adjacent gene expression and for normal meiosis or sporulation. It may be a negative regulator of the telomere-replicating enzyme, telomerase1,3, or may protect against activation of telomerase-independent pathways of telomere elongation8.

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