Human telomerase contains evolutionarily conserved catalytic and structural subunits

  1. Lea Harrington1,3,
  2. Wen Zhou2,
  3. Timothy McPhail2,
  4. Rena Oulton1,
  5. David S.K. Yeung1,
  6. Vernon Mar2,
  7. Michael B. Bass2, and
  8. Murray O. Robinson2,3
  1. 1Amgen Institute/Ontario Cancer Institute, Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2C1, Canada; 2Amgen, Inc., Thousand Oaks, California 91320 USA

Abstract

We have cloned and characterized a human gene encoding TP2 (telomerase-associated protein2), a protein with similarity to reverse transcriptases and the catalytic telomerase subunits from Saccharomyces cerevisiae and Euplotes aediculatus. Indirect immunofluorescence revealed that TP2 was localized to the nucleus. Using antibodies to endogenous and epitope-tagged TP2, we found that TP2 was associated specifically with human telomerase activity and the recently identified telomerase-associated protein TP1. Mutation of conserved residues within the reverse transcriptase domain of TP2 severely reduced associated telomerase activity. These results suggest that telomerase is an evolutionarily conserved multisubunit complex composed of both structural and catalytic subunits.

Keywords

Footnotes

  • 3 Corresponding authors.

  • E-MAIL Leah{at}amgen.com; mrobinso{at}amgen.com; FAX (416) 204-2278.

    • Received August 22, 1997.
    • Accepted September 25, 1997.
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