ArticleNucleic acids research2015
Bacterial initiators form dynamic filaments on single-stranded DNA monomer by monomer.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Assembly of Macromolecular Complexes in the Whole-Cell Model of a Minimal Cell.The journal of physical chemistry. B · 2026Article
- DnaA and SspA regulation of the iraD gene of Escherichia coli: an alternative DNA damage response independent of LexA/RecA.Genetics · 2022Article
- Article
- Interactions of replication initiator RctB with single- and double-stranded DNA in origin opening of Vibrio cholerae chromosome 2.Nucleic acids research · 2020Article
- Mechanisms of Theta Plasmid Replication in Enterobacteria and Implications for Adaptation to Its Host.EcoSal Plus · 2020Review
- Identification of a basal system for unwinding a bacterial chromosome origin.The EMBO journal · 2019Article
- Kinetic Modeling of the Genetic Information Processes in a Minimal Cell.Frontiers in molecular biosciences · 2019Article
- Dynamic stepwise opening of integron attC DNA hairpins by SSB prevents toxicity and ensures functionality.Nucleic acids research · 2017Article
- Review
- The bacterial DnaA-trio replication origin element specifies single-stranded DNA initiator binding.Nature · 2016Article
- Opening the Strands of Replication Origins-Still an Open Question.Frontiers in molecular biosciences · 2016Review
- Replisome Assembly at Bacterial Chromosomes and Iteron Plasmids.Frontiers in molecular biosciences · 2016Review
- Replication Initiation in Bacteria.The EnzymesReview
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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
DNA replication initiation is mediated across all domains of life by initiator proteins oligomerizing at replication origins. Recently, it was shown that initiators can directly bind single-stranded DNA (ssDNA) and thus might enhance origin melting. In this study, we used single-molecule fluorescence assays to probe the ssDNA binding mechanism of the replication initiator DnaA. Our experiments revealed that DnaA forms a dynamic filament on ssDNA in 3' to 5' directionality in the presence of ATP and analogs. After nucleation with a three-monomer seed, monomers dynamically assemble and disassemble one monomer at a time at the 5' end, each monomer binding three nucleotides of ssDNA. The addition of adjacent double-stranded DnaA binding sites stabilized the DnaA filament on ssDNA. Our results extend the current models of origin melting via DnaA ssDNA interaction.
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