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

Autor:	Zemora, Georgeta, Handl, Stefan, Waldsich, Christina
Jazyk:	angličtina
Rok vydání:	2015
Předmět:	enzymes and coenzymes (carbohydrates) RNA Folding HEK293 Cells RNA Stability embryonic structures Mutation RNA Humans Nucleic Acid Conformation biological phenomena cell phenomena and immunity neoplasms Telomerase Protein Binding
Zdroj:	Nucleic Acids Research
ISSN:	1362-4962 0305-1048
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::19d1341e0b387912d9419ec8e28ee47b http://europepmc.org/articles/PMC4705647 Zobrazit plný text záznamu