ArticleNucleic acids research2016
Force and twist dependence of RepC nicking activity on torsionally-constrained DNA molecules.
Article in Nucleic acids research, 2016. 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, 26 citations in OpenAlex.
- KorB switching from DNA-sliding clamp to repressor mediates long-range gene silencing in a multi-drug resistance plasmid.Nature microbiology · 2025Article
- Molecular architecture and oligomerization of Candida glabrata Cdc13 underpin its telomeric DNA-binding and unfolding activity.Nucleic acids research · 2023Article
- Efficient golden gate assembly of DNA constructs for single molecule force spectroscopy and imaging.Nucleic acids research · 2022Article
- Interaction of Proteins with Inverted Repeats and Cruciform Structures in Nucleic Acids.International journal of molecular sciences · 2022Review
- CTP promotes efficient ParB-dependent DNA condensation by facilitating one-dimensional diffusion fromeLife · 2021Article
- Molecular and Functional Characterization of MobK Protein-A Novel-Type Relaxase Involved in Mobilization for Conjugational Transfer ofInternational journal of molecular sciences · 2021Article
- Nanomechanics of G-quadruplexes within the promoter of the KIT oncogene.Nucleic acids research · 2021Article
- Understanding the paradoxical mechanical response of in-phase A-tracts at different force regimes.Nucleic acids research · 2020Article
- Dynamics of DNA nicking and unwinding by the RepC-PcrA complex.Nucleic acids research · 2020Article
- The TubR-centromere complex adopts a double-ring segrosome structure in Type III partition systems.Nucleic acids research · 2018Article
- oriD structure controls RepD initiation during rolling-circle replication.Scientific reports · 2018Article
- Article
- The Different Faces of Rolling-Circle Replication and Its Multifunctional Initiator Proteins.Frontiers in microbiology · 2017Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many bacterial plasmids replicate by an asymmetric rolling-circle mechanism that requires sequence-specific recognition for initiation, nicking of one of the template DNA strands and unwinding of the duplex prior to subsequent leading strand DNA synthesis. Nicking is performed by a replication-initiation protein (Rep) that directly binds to the plasmid double-stranded origin and remains covalently bound to its substrate 5'-end via a phosphotyrosine linkage. It has been proposed that the inverted DNA sequences at the nick site form a cruciform structure that facilitates DNA cleavage. However, the role of Rep proteins in the formation of this cruciform and the implication for its nicking and religation functions is unclear. Here, we have used magnetic tweezers to directly measure the DNA nicking and religation activities of RepC, the replication initiator protein of plasmid pT181, in plasmid sized and torsionally-constrained linear DNA molecules. Nicking by RepC occurred only in negatively supercoiled DNA and was force- and twist-dependent. Comparison with a type IB topoisomerase in similar experiments highlighted a relatively inefficient religation activity of RepC. Based on the structural modeling of RepC and on our experimental evidence, we propose a model where RepC nicking activity is passive and dependent upon the supercoiling degree of the DNA substrate.
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