Open Access

The human telomerase catalytic subunit and viral telomerase RNA reconstitute a functional telomerase complex in a cell-free system, but not in human cells

  • Laetitia Trapp-Fragnet1Email author,
  • Delphine T. Marie-Egyptienne2, 3, 4,
  • Johans Fakhoury2, 5, 6,
  • Denis Rasschaert7 and
  • Chantal Autexier2, 3, 5
Cellular & Molecular Biology LettersAn International Journal201217:31

https://doi.org/10.2478/s11658-012-0031-6

Received: 22 December 2011

Accepted: 28 August 2012

Published: 1 September 2012

Abstract

The minimal vertebrate telomerase enzyme is composed of a protein component (telomerase reverse transcriptase, TERT) and an RNA component (telomerase RNA, TR). Expression of these two subunits is sufficient to reconstitute telomerase activity in vitro, while the formation of a holoenzyme comprising telomerase-associated proteins is necessary for proper telomere length maintenance. Previous reports demonstrated the high processivity of the human telomerase complex and the interspecies compatibility of human TERT (hTERT). In this study, we tested the function of the only known viral telomerase RNA subunit (vTR) in association with human telomerase, both in a cell-free system and in human cells. When vTR is assembled with hTERT in a cell-free environment, it is able to interact with hTERT and to reconstitute telomerase activity. However, in human cells, vTR does not reconstitute telomerase activity and could not be detected in the human telomerase complex, suggesting that vTR is not able to interact properly with the proteins constituting the human telomerase holoenzyme.

Key words

TelomeraseHoloenzymehTERTvTRDyskerinMarek’s disease virus

Notes

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