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TitleStructural basis for dual DNA and RNA specificity of the G-quadruplex-resolving DEAH-box helicase DHX36.
Journal, issue, pagesCell Rep, Vol. 44, Issue 9, Page 116136, Year 2025
Publish dateAug 19, 2025
AuthorsMichael T Banco / Tapas Paul / Jiansen Jiang / Sua Myong / Adrian R Ferré-D'Amaré /
PubMed AbstractDEAH-box helicases, which share a structurally conserved ATPase core, function in all facets of eukaryotic gene expression. While most helicases are highly specialized for their substrates, DHX36 ...DEAH-box helicases, which share a structurally conserved ATPase core, function in all facets of eukaryotic gene expression. While most helicases are highly specialized for their substrates, DHX36 (DEAH-box helicase 36) resolves both DNA and RNA G-quadruplexes. To elucidate the molecular basis of this versatility, we have determined cryo-electron microscopy structures of bovine DHX36 bound to a three-tier RNA G-quadruplex and a six-tier DNA G-quadruplex at 2.6 and 3.4 Å resolution, respectively. Kinetic and smFRET characterizations of structure-guided mutants indicate a key role for the RecA2 domain of the helicase core in DNA vs. RNA discrimination. Furthermore, our structures show that a sequence-divergent RecA2 domain surface loop synergizes with a DHX36-specific N-terminal extension to orthogonally recognize features that specify G-quadruplexes over other nucleic acid structures. Our analysis suggests that recognizing their folded substrates by DEAH-box helicases may generally involve ornamentations of their structural cores acting synergistically with specialized peripheral elements.
External linksCell Rep / PubMed:40833853 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

43612

8vx8

EMDB-43612, PDB-8vx8:
Cryo-EM Structure of DHX36 bound to the cMyc DNA G-quadruplex, Class 1
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • bos taurus (domestic cattle)
  • synthetic construct (others)
KeywordsMOTOR PROTEIN / DEAH-Box Helicase / Helicase / G-quadruplex / RNA

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