Structural basis of G-quadruplex unfolding by the DEAH/RHA helicase DHX36.

ABSTRACT: Guanine-rich nucleic acid sequences challenge the replication, transcription, and translation machinery by spontaneously folding into G-quadruplexes, the unfolding of which requires forces greater than most polymerases can exert^1,2. Eukaryotic cells contain numerous helicases that can unfold G-quadruplexes ³ . The molecular basis of the recognition and unfolding of G-quadruplexes by helicases remains poorly understood. DHX36 (also known as RHAU and G4R1), a member of the DEAH/RHA family of helicases, binds both DNA and RNA G-quadruplexes with extremely high affinity^4-6, is consistently found bound to G-quadruplexes in cells^7,8, and is a major source of G-quadruplex unfolding activity in HeLa cell lysates ⁶ . DHX36 is a multi-functional

SUBMITTER: Chen MC 

PROVIDER: S-EPMC6261253 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature