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Human telomerase reverse transcriptase binds to a pre-organized hTR in vivo exposing its template

About The Author

Dr. Georgeta Zemora studied Biochemistry at the Gene Center, Ludwig Maximilians University, Munich. She completed her PhD in Molecular Biology at the University of Vienna. During her PhD at MFPL Vienna she was guided by her mentor, Dr Christina Waldsich who introduced her into the fascinating field of RNA folding in vivo. Her research focused on deciphering the structure of human telomerase RNA (hTR) in vivo as well as its interaction with the human telomerase reverse transcriptase (hTERT). 

Journal Reference

Nucleic Acids Res. 2016 Jan 8;44(1):413-25.

Zemora G1, Handl S2, Waldsich C2.

Show Affiliations
  1. Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, Dr Bohrgasse 9/5, A-1030 Vienna, Austria [email protected]
  2. Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, Dr Bohrgasse 9/5, A-1030 Vienna, Austria.

Abstract

Telomerase is a specialized reverse transcriptase that is responsible for telomere length maintenance. As in other organisms, the minimal components required for an active human telomerase are the template-providing telomerase RNA (hTR) and the enzymatic entity telomerase reverse transcriptase (hTERT). Here, we explored the structure of hTR and the hTERT-induced conformational changes within hTR in living cells. By employing an in vivo DMS chemical probing technique, we showed that the pseudoknot and associated triple helical scaffold form stably in vivo independently of hTERT. In fact, the dimethyl-sulfate (DMS) modification pattern suggests that hTR alone is capable of adopting a conformation that is suited to interact with hTERT. However, in the absence of hTERT the template region of hTR is only weakly accessible to DMS-modifications. The predominant change after binding of hTERT to hTR is the exposure of the template region.

© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

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