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TitleCryo-EM structures of human FANCJ reveal the mechanism of G-quadruplex unwinding and disease-associated mutations.
Journal, issue, pagesNat Commun, Year 2026
Publish dateJul 15, 2026
AuthorsQinglong You / Naoko Kakusho / Hiroyuki Sasanuma / Hisao Masai / Huilin Li /
PubMed AbstractGuanine-rich nucleic acid sequences can fold into G-quadruplex (G4) structures that regulate DNA replication, transcription, and translation. Fanconi anemia group J helicase (FANCJ) resolves G4 ...Guanine-rich nucleic acid sequences can fold into G-quadruplex (G4) structures that regulate DNA replication, transcription, and translation. Fanconi anemia group J helicase (FANCJ) resolves G4 structures at stalled replication forks. Despite its central role in genome maintenance, the molecular basis of G4 recognition and unwinding by FANCJ has remained unclear. Here, we report cryo-EM structures of human FANCJ bound to a G4-containing DNA substrate and ATPγS. The structures reveal direct engagement of the G4 by the Fe-S domain. Structure-guided mutagenesis demonstrates that this interface is essential for G4 binding and unwinding. The structures further capture open and closed conformational states linked to ATP hydrolysis, providing a mechanism for directional translocation along 5' ssDNA and progressive G4 unwinding. Together, these findings establish the structural basis of G4 recognition by FANCJ and provide mechanistic insights into how disease-associated mutations linked to Fanconi anemia and breast cancer impair helicase function.
External linksNat Commun / PubMed:42457705
MethodsEM (single particle)
Resolution2.8 Å
Structure data

48096

9ej9

EMDB-48096, PDB-9ej9:
Human FANCJ helicase bound to a parallel G4 DNA
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-K:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsISOMERASE/DNA / Helicase / G4 / ISOMERASE-DNA complex

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