Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Brief Communication
  • Published:

Mutation in TERT separates processivity from anchor-site function

Nature Structural & Molecular Biology volume 15, pages 870–872 (2008)Cite this article

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.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

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.

Similar content being viewed by others

References

  1. Lingner, J. et al. Science 276, 561–567 (1997).

    Article  CAS  PubMed  Google Scholar 

  2. Greider, C.W. Mol. Cell. Biol. 11, 4572–4580 (1991).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  3. Hammond, P.W., Lively, T.N. & Cech, T.R. Mol. Cell. Biol. 17, 296–308 (1997).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. Lue, N.F. & Li, Z. Nucleic Acids Res. 35, 5213–5222 (2007).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Jacobs, S.A., Podell, E.R. & Cech, T.R. Nat. Struct. Mol. Biol. 13, 218–225 (2006).

    Article  CAS  PubMed  Google Scholar 

  6. Romi, E. et al. Proc. Natl. Acad. Sci. USA 104, 8791–8796 (2007).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  7. Moriarty, T.J., Marie-Egyptienne, D.T. & Autexier, C. Mol. Cell. Biol. 24, 3720–3733 (2004).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  8. Finger, S.N. & Bryan, T.M. Nucleic Acids Res. 36, 1260–1272 (2008).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  9. Wyatt, H.D., Lobb, D.A. & Beattie, T.L. Mol. Cell. Biol. 27, 3226–3240 (2007).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  10. Miller, M.C., Liu, J.K. & Collins, K. EMBO J. 19, 4412–4422 (2000).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  11. Bar-Nahum, G. et al. Cell 120, 183–193 (2005).

    Article  CAS  PubMed  Google Scholar 

  12. Lai, C.K., Miller, M.C. & Collins, K. Mol. Cell 11, 1673–1683 (2003).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  13. Mason, D.X., Goneska, E. & Greider, C.W. Mol. Cell. Biol. 23, 5606–5613 (2003).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Acknowledgements

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

Author information

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
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Elaine R Podell
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Thomas R Cech
    View author publications

    You can also search for this author in PubMed Google Scholar

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)

Rights and permissions

Reprints and permissions

About this article

Cite this article

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

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsmb.1462

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing