Journal
SCIENTIFIC REPORTS
Volume 4, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep06391
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Categories
Funding
- NIH Director's New Innovator Award [343 NIH 1 DP2 GM105453]
- American Cancer Society [RSG-12-066-01-DMC]
- NIH National Cancer Institute [1F30CA174323-01]
- Linda Su-Nan Chang Sah Doctoral Fellowship
- NIH [R01ES022944]
- David Scaife Foundation
- Division Of Physics
- Direct For Mathematical & Physical Scien [1430124] Funding Source: National Science Foundation
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The ends of eukaryotic chromosomes are capped by telomeres which consist of tandem G-rich DNA repeats stabilized by the shelterin protein complex. Telomeres shorten progressively in most normal cells due to the end replication problem. In more than 85% of cancers however, the telomere length is maintained by telomerase; a reverse transcriptase that adds telomeric TTAGGG repeats using its integral RNA template. The strong association between telomerase activity and malignancy in many cancers suggests that telomerase activity could serve as a diagnostic marker. We demonstrate single-molecule, real-time telomerase extension activity observed digitally as the telomeric repeats are added to a substrate. The human telomerase complex pulled down from mammalian cells displays extension activity dependent on dNTP concentration. In complex with the processivity factor, POT1-TPP1, telomerase adds repeats at an accelerated rate and yields longer products. Our assay provides a unique detection platform that enables the study of telomerase kinetics with single molecule resolution.
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