Pot1, the Putative Telomere End-Binding Protein in Fission Yeast and Humans
Author(s) -
Peter Baumann,
Thomas R. Cech
Publication year - 2001
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.1060036
Subject(s) - telomere , biology , telomere binding protein , genetics , homologous chromosome , chromosome , yeast , dna , schizosaccharomyces pombe , gene , eukaryotic chromosome fine structure , microbiology and biotechnology , dna binding protein , saccharomyces cerevisiae , transcription factor
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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