ArticleThe Journal of biological chemistry2012
Differentiation of the DnaA-oriC subcomplex for DNA unwinding in a replication initiation complex.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Robust helicase loading mechanism underlies diverse architectures of bacterial replication origins.Nucleic acids research · 2026Article
- Adaptive evolution of oriC through in vitro propagation of a mini-chromosome in RCR.Nucleic acids research · 2025Article
- Article
- The bacterial replication origin BUS promotes nucleobase capture.Nature communications · 2023Article
- IHF and Fis asInternational journal of molecular sciences · 2023Review
- Single-stranded DNA recruitment mechanism in replication origin unwinding by DnaA initiator protein and HU, an evolutionary ubiquitous nucleoid protein.Nucleic acids research · 2023Article
- Concerted actions of DnaA complexes with DNA-unwinding sequences within and flanking replication origin oriC promote DnaB helicase loading.The Journal of biological chemistry · 2022Article
- Negative feedback for DARS2-Fis complex by ATP-DnaA supports the cell cycle-coordinated regulation for chromosome replication.Nucleic acids research · 2021Article
- Whole-Genome Analysis Reveals That the Nucleoid Protein IHF Predominantly Binds to the Replication OriginFrontiers in microbiology · 2021Article
- Blocking, Bending, and Binding: Regulation of Initiation of Chromosome Replication During theFrontiers in microbiology · 2021Review
- Interactions of replication initiator RctB with single- and double-stranded DNA in origin opening of Vibrio cholerae chromosome 2.Nucleic acids research · 2020Article
- DnaB helicase is recruited to the replication initiation complex via binding of DnaA domain I to the lateral surface of the DnaB N-terminal domain.The Journal of biological chemistry · 2020Article
- Identification of the Unwinding Region in theFrontiers in microbiology · 2020Article
- A novel mode of DnaA-DnaA interaction promotes ADP dissociation for reactivation of replication initiation activity.Nucleic acids research · 2019Article
- Blocking the Trigger: Inhibition of the Initiation of Bacterial Chromosome Replication as an Antimicrobial Strategy.Antibiotics (Basel, Switzerland) · 2019Review
- Identification of a basal system for unwinding a bacterial chromosome origin.The EMBO journal · 2019Article
- The plasmid-borne quinolone resistance protein QnrB, a novel DnaA-binding protein, increases the bacterial mutation rate by triggering DNA replication stress.Molecular microbiology · 2019Article
- Changing Perspectives on the Role of DnaA-ATP in Orisome Function and Timing Regulation.Frontiers in microbiology · 2019Review
- Lon recognition of the replication initiator DnaA requires a bipartite degron.Molecular microbiology · 2019Article
- Article
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5 authors.
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Abstract
In Escherichia coli, ATP-DnaA multimers formed on the replication origin oriC promote duplex unwinding, which leads to helicase loading. Based on a detailed functional analysis of the oriC sequence motifs, we previously proposed that the left half of oriC forms an ATP-DnaA subcomplex competent for oriC unwinding, whereas the right half of oriC forms a distinct ATP-DnaA subcomplex that facilitates helicase loading. However, the molecular basis for the functional difference between these ATP-DnaA subcomplexes remains unclear. By analyzing a series of novel DnaA mutants, we found that structurally distinct DnaA multimers form on each half of oriC. DnaA AAA+ domain residues Arg-227 and Leu-290 are specifically required for oriC unwinding. Notably, these residues are required for the ATP-DnaA-specific structure of DnaA multimers in complex with the left half of oriC but not for that with the right half. These results support the idea that the ATP-DnaA multimers formed on oriC are not uniform and that they can adopt different conformations. Based on a structural model, we propose that Arg-227 and Leu-290 play a crucial role in inter-ATP-DnaA interaction and are a prerequisite for the formation of unwinding-competent DnaA subcomplexes on the left half of oriC. These residues are not required for the interaction with DnaB, nucleotide binding, or regulatory DnaA-ATP hydrolysis, which further supports their important role in inter-DnaA interaction. The corresponding residues are evolutionarily conserved and are required for unwinding in the initial complexes of Thermotoga maritima, an ancient hyperthermophile. Therefore, our findings suggest a novel and common mechanism for ATP-DnaA-dependent activation of initial complexes.
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