Pot1, the Putative Telomere End-Binding Protein in Fission Yeast and Humans
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 telome...
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Published in | Science (American Association for the Advancement of Science) Vol. 292; no. 5519; pp. 1171 - 1175 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Society for the Advancement of Science
11.05.2001
American Association for the Advancement of Science The American Association for the Advancement of Science |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.1060036 |