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Fission yeast Taz1 protein is required for meiotic telomere clustering and recombination

Abstract

The alignment of homologous chromosomes during meiosis is essential for their recombination and segregation. Telomeres form and protect the ends of eukaryotic linear chromosomes, and are composed of tandem repeats of a simple DNA sequence and the proteins that bind to these repeats1,2,3. A role for telomeres in meiosis was suspected from observations of telomere clustering in meiotic cells4,5,6,7 and has now been supported experimentally by the dramatic rearrangement of telomere locations during premeiotic stages in fission yeast8,9. Here we show that the fission yeast telomere protein, Taz1 (ref. 10), is required for stable association between telomeres and spindle pole bodies during meiotic prophase. In the absence of Taz1, telomere clustering at the spindle pole bodies is disrupted, meiotic recombination is reduced, and both spore viability and the ability of zygotes to re-enter mitosis are impaired to a level that would be expected if chromosome segregation were occurring randomly. Such telomeric association mediated by telomere-specific proteins may also be important for proper chromosome alignment and recombination during meiosis in humans.

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Figure 1: Locations of telomeres and centromeres during meiotic prophase in wild-type and taz1 cells.
Figure 2: Effects of taz1 deletion on telomere clustering, meiotic recombination, spore viability and resumption of mitotic growth.
Figure 3: Taz1 is required for shifts in telomere locations during meiosis in fission yeast.

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Acknowledgements

We thank all the members of our laboratory for discussion, and particularly J. Hayles, J. Mata and K.Sawin for help and advice, K. Ekwall for cosmids, and I. Hagan for anti-Sad1 antibody. J.P.C. was supported by an EMBO fellowship and Y. W. was supported by a JSPS fellowship.

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Correspondence to Julia Promisel Cooper.

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Cooper, J., Watanabe, Y. & Nurse, P. Fission yeast Taz1 protein is required for meiotic telomere clustering and recombination. Nature 392, 828–831 (1998). https://doi.org/10.1038/33947

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