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Pot1, the putative telomere end-binding protein in fission yeast and humans
Pot1, the putative telomere end-binding protein in fission yeast and humans.
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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.
Baumann P, Cech TR
Science (New York, N.Y.)
2001-05-11 00:00
292
5519
1171-5
Amino Acid Sequence,Base Sequence,Binding Sites,Chromosome Segregation,Chromosomes, Fungal,Cloning, Molecular,DNA,DNA-Binding Proteins,Electrophoresis, Gel, Pulsed-Field,Female,Gene Deletion,Gene Expression Profiling,Heterozygote,Humans,Molecular Sequence Data,Ovary,Phenotype,RNA, Messenger,Schizosaccharomyces,Schizosaccharomyces pombe Proteins,Sequence Alignment,Substrate Specificity,Telomere,Telomere-Binding Proteins,DNA-Binding Proteins,POT1 protein, human,RNA, Messenger,Schizosaccharomyces pombe Proteins,Telomere-Binding Proteins,pot1 protein, S pombe,DNA
Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA
Science
0036-8075
10.1126/science.1060036
292/5519/1171
238
True
11349150
