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| The EMBO Journal
(2001) 20, 3526–3534, doi:10.1093/emboj/20.13.3526 |
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| Human telomerase contains two cooperating telomerase RNA molecules |
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| Christian Wenz1, Barbara Enenkel2, Mario Amacker1, Colleen Kelleher1, Klaus Damm2 and Joachim Lingner1 |
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1 Swiss Institute for Experimental Cancer Research (ISREC), CH-1066 Epalinges, Switzerland 2 Boehringer-Ingelheim Pharma KG, D-88397 Biberach a. d. Riss, Germany To whom correspondence should be addressed Joachim Lingner, joachim.lingner@isrec.unil.ch Received 3 April 2001; Revised 4 May 2001; Accepted 10 May 2001. |
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| Abstract |
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| Telomerase uses a short stretch of its intrinsic RNA molecule as template for telomere repeat synthesis. Reverse transcription of the RNA template is catalyzed by the telomerase reverse transcriptase (TERT) protein subunit. We demonstrate that human telomerase reconstituted from recombinant TERT and telomerase RNA runs as a dimer on a gel filtration column and that it contains two telomerase RNA molecules. Significantly, a telomerase heterodimer reconstituted from wild-type and mutant telomerase RNA is barely active when compared with the wild-type homodimer. We conclude that the telomerase RNA templates in the active enzyme are interdependent and functionally cooperate with each other. We discuss models that may explain the biological and enzymatic roles of telomerase dimerization. |
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| Keywords: dimer, reverse transcriptase, ribonucleoprotein, telomerase, telomere |
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