ArticleNature chemical biology2015
Strand separation establishes a sustained lock at the Tus-Ter replication fork barrier.
Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- MTERF1 polar roadblock mechanism revealed using high-throughput magnetic tweezers and accurate single-bead force calibration.Nucleic acids research · 2026Article
- Termination of DNA replication drives genomic instability via multiple mechanisms.Nucleic acids research · 2026Article
- Interplay between chromosomal architecture and termination of DNA replication in bacteria.Frontiers in microbiology · 2023Review
- A modified CUT&RUN-seq technique for qPCR analysis of chromatin-protein interactions.STAR protocols · 2022Article
- Delineation of the Ancestral Tus-Dependent Replication Fork Trap.International journal of molecular sciences · 2021Article
- Dynamics and inhibition of MLL1 CXXC domain on DNA revealed by single-molecule quantification.Biophysical journal · 2021Article
- Dynamics of TRF1 organizing a single human telomere.Nucleic acids research · 2021Article
- Review
- Temperature controlled high-throughput magnetic tweezers show striking difference in activation energies of replicating viral RNA-dependent RNA polymerases.Nucleic acids research · 2020Article
- High-yield fabrication of DNA and RNA constructs for single molecule force and torque spectroscopy experiments.Nucleic acids research · 2019Article
- Rescuing Replication from Barriers: Mechanistic Insights from Single-Molecule Studies.Molecular and cellular biology · 2019Review
- Signatures of Nucleotide Analog Incorporation by an RNA-Dependent RNA Polymerase Revealed Using High-Throughput Magnetic Tweezers.Cell reports · 2017Article
- Single molecule high-throughput footprinting of small and large DNA ligands.Nature communications · 2017Article
- Review
- Watching cellular machinery in action, one molecule at a time.The Journal of cell biology · 2017Review
- The progression of replication forks at natural replication barriers in live bacteria.Nucleic acids research · 2016Article
- Replication Termination: Containing Fork Fusion-Mediated Pathologies in Escherichia coli.Genes · 2016Review
- DNA replication: Unlocking the secrets of fork arrest.Nature chemical biology · 2015Article
- Single-molecule multiplexed profiling of protein-DNA complexes using magnetic tweezers.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bidirectional replication of a circular chromosome by many bacteria necessitates proper termination to avoid the head-on collision of the opposing replisomes. In Escherichia coli, replisome progression beyond the termination site is prevented by Tus proteins bound to asymmetric Ter sites. Structural evidence indicates that strand separation on the blocking (nonpermissive) side of Tus-Ter triggers roadblock formation, but biochemical evidence also suggests roles for protein-protein interactions. Here DNA unzipping experiments demonstrate that nonpermissively oriented Tus-Ter forms a tight lock in the absence of replicative proteins, whereas permissively oriented Tus-Ter allows nearly unhindered strand separation. Quantifying the lock strength reveals the existence of several intermediate lock states that are impacted by mutations in the lock domain but not by mutations in the DNA-binding domain. Lock formation is highly specific and exceeds reported in vivo efficiencies. We postulate that protein-protein interactions may actually hinder, rather than promote, proper lock formation.
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Registered trials
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.