ArticleThe Journal of biological chemistry2015
The Arg Fingers of Key DnaA Protomers Are Oriented Inward within the Replication Origin oriC and Stimulate DnaA Subcomplexes in the Initiation Complex.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 41 citations in OpenAlex.
- Robust helicase loading mechanism underlies diverse architectures of bacterial replication origins.Nucleic acids research · 2026Article
- Dynamic DnaA-DnaB interactions at oriC coordinate the loading and coupled translocation of two DnaB helicases for bidirectional replication.Nucleic acids research · 2026Article
- The iron-sulfur accelerator YgfZ modulates genome-wide IHF-binding dynamics to regulate replication initiation inFrontiers in microbiology · 2026Article
- The Escherichia coli replication initiator DnaA is titrated on the chromosome.Nature communications · 2025Article
- Article
- Negative DNA supercoiling enhances DARS2 binding of DNA-bending protein IHF in the activation of Fis-dependent ATP-DnaA production.Nucleic acids research · 2025Article
- Read-through transcription of tRNA underlies the cell cycle-dependent dissociation of IHF from the DnaA-inactivating sequenceFrontiers in microbiology · 2024Article
- 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
- Putative Cooperative ATP-DnaA Binding to Double-Stranded DnaA Box and Single-Stranded DnaA-Trio Motif uponInternational journal of molecular sciences · 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
- 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
- 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
- Changing Perspectives on the Role of DnaA-ATP in Orisome Function and Timing Regulation.Frontiers in microbiology · 2019Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ATP-DnaA binds to multiple DnaA boxes in the Escherichia coli replication origin (oriC) and forms left-half and right-half subcomplexes that promote DNA unwinding and DnaB helicase loading. DnaA forms homo-oligomers in a head-to-tail manner via interactions between the bound ATP and Arg-285 of the adjacent protomer. DnaA boxes R1 and R4 reside at the outer edges of the DnaA-binding region and have opposite orientations. In this study, roles for the protomers bound at R1 and R4 were elucidated using chimeric DnaA molecules that had alternative DNA binding sequence specificity and chimeric oriC molecules bearing the alternative DnaA binding sequence at R1 or R4. In vitro, protomers at R1 and R4 promoted initiation regardless of whether the bound nucleotide was ADP or ATP. Arg-285 was shown to play an important role in the formation of subcomplexes that were active in oriC unwinding and DnaB loading. The results of in vivo analysis using the chimeric molecules were consistent with the in vitro data. Taken together, the data suggest a model in which DnaA subcomplexes form in symmetrically opposed orientations and in which the Arg-285 fingers face inward to mediate interactions with adjacent protomers. This mode is consistent with initiation regulation by ATP-DnaA and bidirectional loading of DnaB helicases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.