title: Single-molecule analysis of human telomerase monomer.
abstract: 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.
authors.affiliation: University Chemical Laboratories, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
authors.forename: David
authors.initials: D
authors.lastname: Alves
authors.forename: Haitao
authors.initials: H
authors.lastname: Li
authors.forename: Rosalind
authors.initials: R
authors.lastname: Codrington
authors.forename: Angel
authors.initials: A
authors.lastname: Orte
authors.forename: Xiaojun
authors.initials: X
authors.lastname: Ren
authors.forename: David
authors.initials: D
authors.lastname: Klenerman
authors.forename: Shankar
authors.initials: S
authors.lastname: Balasubramanian
mesh_terms: D002384:Catalysis; D005453:Fluorescence; D006801:Humans; D013379:Substrate Specificity; D019098:Telomerase / Q000737:chemistry* / Q000378:metabolism
chemical_list: C509186:TERT protein, human; D019098:Telomerase