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TitleDnaB and DciA: mechanisms of helicase loading and translocation on ssDNA.
Journal, issue, pagesNucleic Acids Res, Vol. 53, Issue 12, Year 2025
Publish dateJun 20, 2025
AuthorsNicholas Gao / Daniele Mazzoletti / Adele Peng / Paul Dominic B Olinares / Castrese Morrone / Andrea Garavaglia / Nourelhoda Gouda / Sergey Tsoy / Albert Mendoza / Ahammad Chowdhury / Antonio Cerullo / Hrutvik Bhavsar / Franca Rossi / Menico Rizzi / Brian T Chait / Riccardo Miggiano / David Jeruzalmi /
PubMed AbstractReplicative helicases are assembled on chromosomes by helicase loaders before the initiation of DNA replication. Here, we investigate the mechanisms employed by the bacterial Vibrio cholerae (Vc) ...Replicative helicases are assembled on chromosomes by helicase loaders before the initiation of DNA replication. Here, we investigate the mechanisms employed by the bacterial Vibrio cholerae (Vc) DnaB replicative helicase and the DciA helicase loader. Structural analysis of the ATPγS form of the VcDnaB-ssDNA complex reveals a configuration distinct from that observed with GDP•AlF4. With ATPγS, the amino-terminal domain (NTD) tier, previously found as an open spiral in the GDP•AlF4 complex, adopts a closed planar arrangement. Furthermore, the DnaB subunit at the top of the carboxy-terminal domain (CTD) spiral is displaced by approximately 25 Å between the two forms. We suggest that remodeling the NTD layer between closed planar and open spiral configurations, along with the migration of two distinct CTDs to the top of the DnaB spiral, repeated three times, mediates hand-over-hand translocation. Biochemical analysis indicates that VcDciA utilizes its Lasso domain to interact with DnaB near its Docking-Helix Linker-Helix interface. Up to three copies of VcDciA bind to VcDnaB, suppressing its ATPase activity during loading onto physiological DNA substrates. Our data suggest that DciA loads DnaB onto DNA using the ring-opening mechanism.
External linksNucleic Acids Res / PubMed:40598899 / PubMed Central
MethodsEM (single particle)
Resolution3.37 Å
Structure data

46984

9dls

EMDB-46984, PDB-9dls:
Vibrio cholerae DnaB
Method: EM (single particle) / Resolution: 3.37 Å

Chemicals

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

ChemComp-MG:
Unknown entry

Source
  • vibrio cholerae o1 (bacteria)
  • vibrio cholerae (bacteria)
KeywordsDNA BINDING PROTEIN/DNA / Replicative Helicase / DNA Replication / Vibrio cholerae / Helicase Loading / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex

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