ArticleThe Journal of biological chemistry2009
Strand displacement by DNA polymerase III occurs through a tau-psi-chi link to single-stranded DNA-binding protein coating the lagging strand template.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 52 citations in OpenAlex.
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- DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026Review
- ATP is dispensable for E. coli DNA replication and eukaryotic helicase activity.Nature communications · 2026Article
- Mechanisms of chromosomal DNA replication in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2026Review
- nCas9-based method for rolling-circle DNA substrate generation.Analytical biochemistry · 2025Article
- A four-point molecular handover during Okazaki maturation.Nature structural & molecular biology · 2023Article
- Mechanism of strand displacement DNA synthesis by the coordinated activities of human mitochondrial DNA polymerase and SSB.Nucleic acids research · 2023Article
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
- The Impact of RNA-DNA Hybrids on Genome Integrity in Bacteria.Annual review of microbiology · 2022Review
- Quantitative methods to study helicase, DNA polymerase, and exonuclease coupling during DNA replication.Methods in enzymology · 2022Article
- Bypass of complex co-directional replication-transcription collisions by replisome skipping.Nucleic acids research · 2021Article
- Replisome bypass of transcription complexes and R-loops.Nucleic acids research · 2020Article
- A Primase-Induced Conformational Switch Controls the Stability of the Bacterial Replisome.Molecular cell · 2020Article
- Development of a single-stranded DNA-binding protein fluorescent fusion toolbox.Nucleic acids research · 2020Article
- Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mechanisms of bacterial DNA replication restart.Nucleic acids research · 2018Review
- Collision with duplex DNA renders Escherichia coli DNA polymerase III holoenzyme susceptible to DNA polymerase IV-mediated polymerase switching on the sliding clamp.Scientific reports · 2017Article
- Methods to study the coupling between replicative helicase and leading-strand DNA polymerase at the replication fork.Methods (San Diego, Calif.) · 2016Review
- DNA Polymerase III, but Not Polymerase IV, Must Be Bound to a τ-Containing DnaX Complex to Enable Exchange into Replication Forks.The Journal of biological chemistry · 2016Article
- Transcriptomic and Metabolomic Analysis Revealed Multifaceted Effects of Phage Protein Gp70.1 onFrontiers in microbiology · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In addition to the well characterized processive replication reaction catalyzed by the DNA polymerase III holoenzyme on single-stranded DNA templates, the enzyme possesses an intrinsic strand displacement activity on flapped templates. The strand displacement activity is distinguished from the single-stranded DNA-templated reaction by a high dependence upon single-stranded DNA binding protein and an inability of gamma-complex to support the reaction in the absence of tau. However, if gamma-complex is present to load beta(2), a truncated tau protein containing only domains III-V will suffice. This truncated protein is sufficient to bind both the alpha subunit of DNA polymerase (Pol) III and chipsi. This is reminiscent of the minimal requirements for Pol III to replicate short single-stranded DNA-binding protein (SSB)-coated templates where tau is only required to serve as a scaffold to hold Pol III and chi in the same complex (Glover, B., and McHenry, C. (1998) J. Biol. Chem. 273, 23476-23484). We propose a model in which strand displacement by DNA polymerase III holoenzyme depends upon a Pol III-tau-psi-chi-SSB binding network, where SSB is bound to the displaced strand, stabilizing the Pol III-template interaction. The same interaction network is probably important for stabilizing the leading strand polymerase interactions with authentic replication forks. The specificity constant (k(cat)/K(m)) for the strand displacement reaction is approximately 300-fold less favorable than reactions on single-stranded templates and proceeds with a slower rate (150 nucleotides/s) and only moderate processivity (approximately 300 nucleotides). PriA, the initiator of replication restart on collapsed or misassembled replication forks, blocks the strand displacement reaction, even if added to an ongoing reaction.
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