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Related Experiment Videos

Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling.

Jan P Erzberger1, Melissa L Mott, James M Berger

  • 1Division of Biochemistry and Molecular Biology, Molecular and Cell Biology Department, 327B Hildebrand Hall #3206, University of California, Berkeley, California 94720, USA.

Nature Structural & Molecular Biology
|July 11, 2006
PubMed
Summary

Bacterial DNA replication initiation protein DnaA forms a superhelix, enabling DNA unwinding. This AAA+ protein structure is conserved across life, revealing a universal mechanism for replication origins.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Bacterial DNA replication initiation is regulated by the DnaA protein, a key member of the ATPases associated with various cellular activities (AAA+) superfamily.
  • DnaA transitions from a monomer to an oligomeric complex upon ATP binding, remodeling replication origins, melting DNA duplexes, and facilitating replisome assembly.

Purpose of the Study:

  • To elucidate the structural basis of DnaA's function in bacterial replication initiation.
  • To understand how DnaA interacts with DNA and facilitates origin unwinding.
  • To explore the evolutionary conservation of AAA+ initiator structures.

Main Methods:

  • X-ray crystallography of AMP-PCP-bound DnaA.
  • Topology footprint assays to study DNA-protein interactions.

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Main Results:

  • The crystal structure revealed a right-handed superhelix in DnaA, driven by protein-ATP interactions.
  • Topology footprint assays confirmed a right-handed DNA wrap around the DnaA initiation complex.
  • Structural elements promoting open-helix formation are conserved in eukaryotic and archaeal initiators.

Conclusions:

  • A right-handed DNA wrap model explains DnaA's mechanism for engaging and unwinding bacterial replication origins.
  • AAA+ proteins likely engage DnaA at filament ends for regulation.
  • A spiral, open-ring AAA+ assembly represents a conserved core structure for replication initiators across all domains of life.