ArticleThe Journal of biological chemistry2013
The human Tim-Tipin complex interacts directly with DNA polymerase epsilon and stimulates its synthetic activity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Two fork protection complexes at the replication fork play distinct roles in fork progression and stress response.Research square · 2026Article
- A new model for coordinating the functions of TIMELESS at the replication fork.bioRxiv : the preprint server for biology · 2025Article
- Timeless-Tipin interactions with MCM and RPA mediate DNA replication stress response.Frontiers in cell and developmental biology · 2024Article
- The TIMELESS effort for timely DNA replication and protection.Cellular and molecular life sciences : CMLS · 2023Review
- Separable functions of Tof1/Timeless in intra-S-checkpoint signalling, replisome stability and DNA topological stress.Nucleic acids research · 2020Article
- Interaction of the Warsaw breakage syndrome DNA helicase DDX11 with the replication fork-protection factor Timeless promotes sister chromatid cohesion.PLoS genetics · 2018Article
- The DNA Pol ϵ stimulatory activity of Mrc1 is modulated by phosphorylation.Cell cycle (Georgetown, Tex.) · 2018Article
- Tim/Timeless, a member of the replication fork protection complex, operates with the Warsaw breakage syndrome DNA helicase DDX11 in the same fork recovery pathway.Nucleic acids research · 2016Article
- Yeast DNA polymerase ϵ catalytic core and holoenzyme have comparable catalytic rates.The Journal of biological chemistry · 2015Article
- Architecture and ssDNA interaction of the Timeless-Tipin-RPA complex.Nucleic acids research · 2014Article
- Tipin functions in the protection against topoisomerase I inhibitor.The Journal of biological chemistry · 2014Article
- Mta2 promotes Tipin-dependent maintenance of replication fork integrity.Cell cycle (Georgetown, Tex.) · 2014Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Tim-Tipin complex plays an important role in the S phase checkpoint and replication fork stability in metazoans, but the molecular mechanism underlying its biological function is poorly understood. Here, we present evidence that the recombinant human Tim-Tipin complex (and Tim alone) markedly enhances the synthetic activity of DNA polymerase ε. In contrast, no significant effect on the synthetic ability of human DNA polymerase α and δ by Tim-Tipin was observed. Surface plasmon resonance measurements and co-immunoprecipitation experiments revealed that recombinant DNA polymerase ε directly interacts with either Tim or Tipin. In addition, the results of DNA band shift assays suggest that the Tim-Tipin complex (or Tim alone) is able to associate with DNA polymerase ε bound to a 40-/80-mer DNA ligand. Our results are discussed in view of the molecular dynamics at the human DNA replication fork.
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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.