Brief Communication abstract
Nature Chemical Biology 4, 287 - 289 (2008)
Published online: 6 April 2008 | Corrected online: 1 May 2008 | doi:10.1038/nchembio.82
There is an Erratum (June 2008) associated with this Brief Communication.
Single-molecule analysis of human telomerase monomer
David Alves1,2, Haitao Li1,2, Rosalind Codrington1, Angel Orte1, Xiaojun Ren1, David Klenerman1 & Shankar Balasubramanian1
Human telomerase is a ribonucleoprotein that is minimally comprised of protein (hTERT) and RNA (hTR) components. We have applied single-molecule fluorescence two-color coincidence detection to characterize complex formation between fluorophore-labeled components in solution. By systematic labeling and in vitro assembly of hTERT, hTR and telomerase's DNA substrate, we have established that catalytically functional human telomerase comprises a stable hTERT:hTR:substrate interaction in a 1:1:1 absolute stoichiometry.
- University Chemical Laboratories, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
- These authors contributed equally to this work.
Correspondence to: Shankar Balasubramanian1 e-mail: sb10031@cam.ac.uk
Correspondence to: David Klenerman1 e-mail: dk10012@cam.ac.uk
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