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.

There is an Erratum (June 2008) associated with this Brief Communication.

There is an Erratum (June 2008) associated with this Brief Communication.

There is an Erratum (June 2008) associated with this Brief Communication.

There is an Erratum (June 2008) associated with this Brief Communication.

There is an Erratum (June 2008) associated with this Brief Communication.

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

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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.

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  1. University Chemical Laboratories, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
  2. 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

* In the version of this article initially published, parentheses were missing around covalently attached domains in fusion proteins. Also, in the first two lines of the left column of page 288, "hTERT-YFP" should have read "YFP-hTERT" for consistency with the rest of the manuscript. The errors have been corrected in the HTML and PDF versions of the article.

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