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Transcriptional activity of telomerase complex in CD34minus stem cells of cord blood in dependence of preparation time

100%

Stojko R. , Witek A. , Glogowska-Lingus J. , Mazurek U. , Chromy G. , Dworzecki T. , Bojdys-Szyndlar M. , Machaj K. , Pojda Z.

Folia Histochemica et Cytobiologica

2009

tom 47

nr 2

265-274

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

67%

Trapp-Fragnet L. , Marie-Egyptienne D. T. , Fakhoury J. , Rasschaert D. , Autexier C.

Cellular and Molecular Biology Letters

2012

tom 17

nr 4

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.