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Pot1, the putative telomere end-binding protein in fission yeast and humans.
Baumann, P; Cech, T R.
Affiliation
  • Baumann P; Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Science ; 292(5519): 1171-5, 2001 May 11.
Article in En | MEDLINE | ID: mdl-11349150
ABSTRACT
Telomere proteins from ciliated protozoa bind to the single-stranded G-rich DNA extensions at the ends of macronuclear chromosomes. We have now identified homologous proteins in fission yeast and in humans. These Pot1 (protection of telomeres) proteins each bind the G-rich strand of their own telomeric repeat sequence, consistent with a direct role in protecting chromosome ends. Deletion of the fission yeast pot1+ gene has an immediate effect on chromosome stability, causing rapid loss of telomeric DNA and chromosome circularization. It now appears that the protein that caps the ends of chromosomes is widely dispersed throughout the eukaryotic kingdom.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Schizosaccharomyces / Telomere / Telomere-Binding Proteins / DNA-Binding Proteins Type of study: Prognostic_studies Limits: Female / Humans Language: En Journal: Science Year: 2001 Type: Article Affiliation country: United States
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Collection: 01-internacional Database: MEDLINE Main subject: Schizosaccharomyces / Telomere / Telomere-Binding Proteins / DNA-Binding Proteins Type of study: Prognostic_studies Limits: Female / Humans Language: En Journal: Science Year: 2001 Type: Article Affiliation country: United States