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Science 11 May 2001:
Vol. 292. no. 5519, pp. 1171 - 1175
DOI: 10.1126/science.1060036
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Reports

Pot1, the Putative Telomere End-Binding Protein in Fission Yeast and Humans

Peter Baumann, Thomas R. Cech*

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 (<UNL>p</UNL>rotection <UNL>o</UNL>f <UNL>t</UNL>elomeres) 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.

Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
*   To whom correspondence should be addressed. E-mail: thomas.cech{at}colorado.edu

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   Abstract »    Full Text »    PDF »
Resistance to the Short Term Antiproliferative Activity of the G-quadruplex Ligand 12459 Is Associated with Telomerase Overexpression and Telomere Capping Alteration.
D. Gomez, N. Aouali, A. Londono-Vallejo, L. Lacroix, F. Megnin-Chanet, T. Lemarteleur, C. Douarre, K. Shin-ya, P. Mailliet, C. Trentesaux, et al. (2003)
J. Biol. Chem. 278, 50554-50562
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Science. ISSN 0036-8075 (print), 1095-9203 (online)