Regulation of telomere length and function by a Myb-domain protein in fission yeast - PubMed (original) (raw)

. 1997 Feb 20;385(6618):744-7.

doi: 10.1038/385744a0.

Affiliations

• PMID: 9034194
• DOI: 10.1038/385744a0

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

J P Cooper et al. Nature. 1997.

Abstract

Telomeres, the specialized nucleoprotein structures that comprise the ends of eukaryotic chromosomes, are essential for complete replication, and regulation of their length has been a focus of research on tumorigenesis. In the budding yeast Saccharomyces cerevisiae, the protein Rap1p binds to telomeric DNA and functions in the regulation of telomere length. A human telomere protein, hTRF (human TTAGGG repeat factor) binds the telomere sequence in vitro and localizes to telomeres cytologically, but its functions are not yet known. Here we use a genetic screen to identify a telomere protein in fission yeast, Taz1p (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. Taz1p 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, telomerase, or may protect against activation of telomerase-independent pathways of telomere elongation.

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Comment in

• Telomeres. Different means to common ends.
  Shore D. Shore D. Nature. 1997 Feb 20;385(6618):676-7. doi: 10.1038/385676a0. Nature. 1997. PMID: 9034181 No abstract available.

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