Single-molecule FRET-Rosetta reveals RNA structural rearrangements during human telomerase catalysis.

ABSTRACT: Maintenance of telomeres by telomerase permits continuous proliferation of rapidly dividing cells, including the majority of human cancers. Despite its direct biomedical significance, the architecture of the human telomerase complex remains unknown. Generating homogeneous telomerase samples has presented a significant barrier to developing improved structural models. Here we pair single-molecule Förster resonance energy transfer (smFRET) measurements with Rosetta modeling to map the conformations of the essential telomerase RNA core domain within the active ribonucleoprotein. FRET-guided modeling places the essential pseudoknot fold distal to the active site on a protein surface comprising the C-terminal element, a domain that shares structural homology with canonical polymerase thumb doma

SUBMITTER: Parks JW 

PROVIDER: S-EPMC5238793 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature