DNA stretching by bacterial initiators promotes replication origin opening
Copyright policy )DNA stretching by bacterial initiators promotes replication origin opening
Many replication initiators form higher-order oligomers that process host replication origins to promote replisome formation. In addition to dedicated duplex-DNA-binding domains, cellular initiators possess AAA+ (ATPases associated with various cellular activities) elements that drive functions ranging from protein assembly to origin recognition. In bacteria, the AAA+ domain of the initiator DnaA has been proposed to assist in single-stranded DNA formation during origin melting. Here we show crystallographically and in solution that the ATP-dependent assembly of Aquifex aeolicus DnaA into a spiral oligomer creates a continuous surface that allows successive AAA+ domains to bind and extend single-stranded DNA segments. The mechanism of binding is unexpectedly similar to that of RecA, a homologous recombination factor, but it differs in that DnaA promotes a nucleic acid conformation that prevents pairing of a complementary strand. These findings, combined with strand-displacement assays, indicate that DnaA opens replication origins by a direct ATP-dependent stretching mechanism. Comparative studies reveal notable commonalities between the approach used by DnaA to engage DNA substrates and other, nucleic-acid-dependent, AAA+ systems.
- University of California System United States
- University of California, Berkeley United States
- University of California at Berkeley, Department of Molecular and Cell Biology United States
- UNIVERSITY OF CALIFORNIA BERKELEY
- University of California, San Francisco United States
Adenosine Triphosphatases, DNA Replication, DNA, Bacterial, Models, Molecular, Bacteria, Molecular Conformation, DNA, Single-Stranded, Replication Origin, DNA-Directed DNA Polymerase, Crystallography, X-Ray, Nucleic Acid Denaturation, AT Rich Sequence, Article, Substrate Specificity, DNA-Binding Proteins, Rec A Recombinases, Adenosine Triphosphate, Bacterial Proteins, Multienzyme Complexes, Biocatalysis, Nucleic Acid Conformation
Adenosine Triphosphatases, DNA Replication, DNA, Bacterial, Models, Molecular, Bacteria, Molecular Conformation, DNA, Single-Stranded, Replication Origin, DNA-Directed DNA Polymerase, Crystallography, X-Ray, Nucleic Acid Denaturation, AT Rich Sequence, Article, Substrate Specificity, DNA-Binding Proteins, Rec A Recombinases, Adenosine Triphosphate, Bacterial Proteins, Multienzyme Complexes, Biocatalysis, Nucleic Acid Conformation
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