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A more recent version of this article appeared on July 1, 2004
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Submitted on March 9, 2004
Revised on April 14, 2004
Accepted on April 21, 2004
1 Ontario Cancer Institute/Advanced Medical Discovery Institute, Department of Medical Biophysics, University of Toronto, 620 University Avenue, Suite 706, Toronto, Ontario M5G 2C1 Canada
* Corresponding author. E-mail address: leah{at}uhnres.utoronto.ca.
Ciliate and yeast telomerase possess a nucleolytic activity capable of removing DNA from the 3' end of a single-stranded oligonucleotide substrate. The nuclease activity is thought to assist in enzyme proofreading and/or processivity. Herein we report a previously uncharacterized human telomerase-associated nuclease activity that shares several properties with ciliate and yeast telomerases. Partially purified human telomerase, either from cell extracts or recombinantly produced, demonstrated an ability to remove 3' nontelomeric nucleotides from a substrate containing 5' telomeric DNA, followed by extension of the newly exposed telomeric sequence. This cleavage/extension activity was apparent at more than one position within the telomeric DNA, and was influenced by sequences 5' to the telomeric/nontelomeric boundary, and by substitution with a methylphosphonate moiety at the telomeric/nontelomeric DNA boundary. Our data suggest that human telomerase is associated with an evolutionarily conserved nucleolytic activity and support a model in which telomerase-substrate interactions occur distal from the 3' primer end.
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