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Structure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assembly

Author

Listed:
  • Bin Liu

    (Yale University
    Howard Hughes Medical Institute)

  • William K. Eliason

    (Yale University
    Howard Hughes Medical Institute)

  • Thomas A. Steitz

    (Yale University
    Howard Hughes Medical Institute
    Yale University)

Abstract

During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC DNA and then dissociate from the complex. Here, to provide a better understanding of this key process, we report the crystal structure of the ~570-kDa prepriming complex between the Bacillus subtilis loader protein and the Bacillus stearothermophilus helicase, as well as the helicase-binding domain of primase with a molar ratio of 6:6:3 at 7.5 Å resolution. The overall architecture of the complex exhibits a three-layered ring conformation. Moreover, the structure combined with the proposed model suggests that the shift from the ‘open-ring’ to the ‘open-spiral’ and then the ‘closed-spiral’ state of the helicase ring due to the binding of single-stranded DNA may be the cause of the loader release.

Suggested Citation

  • Bin Liu & William K. Eliason & Thomas A. Steitz, 2013. "Structure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assembly," Nature Communications, Nature, vol. 4(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3495
    DOI: 10.1038/ncomms3495
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    Cited by:

    1. Xiang Feng & Michelle M. Spiering & Ruda Luna Almeida Santos & Stephen J. Benkovic & Huilin Li, 2023. "Structural basis of the T4 bacteriophage primosome assembly and primer synthesis," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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