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

Jan P. Erzberger, Melissa L. Mott, James M Berger

Research output: Contribution to journalArticle

Abstract

In bacteria, the initiation of replication is controlled by DnaA, a member of the ATPases associated with various cellular activities (AAA+) protein superfamily. ATP binding allows DnaA to transition from a monomeric state into a large oligomeric complex that remodels replication origins, triggers duplex melting and facilitates replisome assembly. The crystal structure of AMP-PCP-bound DnaA reveals a right-handed superhelix defined by specific protein-ATP interactions. The observed quaternary structure of DnaA, along with topology footprint assays, indicates that a right-handed DNA wrap is formed around the initiation nucleoprotein complex. This model clarifies how DnaA engages and unwinds bacterial origins and suggests that additional, regulatory AAA+ proteins engage DnaA at filament ends. Eukaryotic and archaeal initiators also have the structural elements that promote open-helix formation, indicating that a spiral, open-ring AAA+ assembly forms the core element of initiators in all domains of life.

Original languageEnglish (US)
Pages (from-to)676-683
Number of pages8
JournalNature structural & molecular biology
Volume13
Issue number8
DOIs
StatePublished - Aug 2006
Externally publishedYes

Fingerprint

Replication Origin
Adenosine Triphosphate
Proteins
Nucleoproteins
Freezing
Adenosine Triphosphatases
Bacteria
DNA

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. / Erzberger, Jan P.; Mott, Melissa L.; Berger, James M.

In: Nature structural & molecular biology, Vol. 13, No. 8, 08.2006, p. 676-683.

Research output: Contribution to journalArticle

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