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Mutation in TERT separates processivity from anchor-site function

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Abstract

Telomerase shows repeat-addition processivity (RAP): synthesis of multiple telomeric DNA repeats without primer dissociation. Leu14 mutants in the telomerase essential N-terminal domain of Tetrahymena thermophila telomerase reverse transcriptase retain full activity and anchor-site function but lose RAP, suggesting models for how this domain facilitates DNA translocation.

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Figure 1: Leu14 mutants of Tetrahymena TERT have a specific defect in RAP.
Figure 2: L14A mutation does not disrupt the anchor site.
Figure 3: Model.

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Acknowledgements

We thank K. Collins, N. Lue and A. Berman for useful discussions.

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Authors and Affiliations

  1. Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309-0215, USA.,

    Arthur J Zaug, Elaine R Podell & Thomas R Cech

Authors
  1. Arthur J Zaug
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  2. Elaine R Podell
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  3. Thomas R Cech
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Contributions

A.J.Z. made the initial discovery and designed and carried out experiments; E.R.P. contributed to data analysis and interpretation; T.R.C. contributed to experimental design and models.

Corresponding authors

Correspondence to Arthur J Zaug or Thomas R Cech.

Supplementary information

Supplementary Text and Figures

Supplementary Figures 1–6, Supplementary Methods and Supplementary Discussion (PDF 1581 kb)

Supplementary Movie

Leu14 (shown as the branched amino acid) acts as a latch between the TEN domain and the remainder of telomerase, opening and closing during the reaction cycle. See Figure 3 in the main text for details. (MOV 9167 kb)

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Zaug, A., Podell, E. & Cech, T. Mutation in TERT separates processivity from anchor-site function. Nat Struct Mol Biol 15, 870–872 (2008). https://doi.org/10.1038/nsmb.1462

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