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• W1825955700 endingPage "425" @default.
• W1825955700 startingPage "413" @default.
• W1825955700 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." @default.
• W1825955700 created "2016-06-24" @default.
• W1825955700 creator A5013239958 @default.
• W1825955700 creator A5029744321 @default.
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• W1825955700 date "2015-10-19" @default.
• W1825955700 modified "2023-10-17" @default.
• W1825955700 title "Human telomerase reverse transcriptase binds to a pre-organized hTR<i>in vivo</i>exposing its template" @default.
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• W1825955700 doi "https://doi.org/10.1093/nar/gkv1065" @default.
• W1825955700 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4705647" @default.
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• W1825955700 hasPublicationYear "2015" @default.
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