ArticleJournal of bacteriology2021
Genetic Analysis of DinG Family Helicase YoaA and Its Interaction with Replication Clamp Loader Protein HolC in Escherichia coli.
Article in Journal of bacteriology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 8 citations in OpenAlex.
- Structural and biochemical characterization of a novel DinG containing an endonuclease domain.Cellular and molecular life sciences : CMLS · 2026Article
- A novel ψ-χ fusion protein for unravelling the contributions of χ to DNA replication and repair.Nucleic acids research · 2026Article
- A NovelbioRxiv : the preprint server for biology · 2026Article
- Article
- The YoaA-χ helicase modulates the dynamics of single-stranded DNA binding protein on DNA.Nature communications · 2025Article
- Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025Review
- The DNA damage response ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Single-stranded DNA binding protein hitches a ride with thebioRxiv : the preprint server for biology · 2024Article
- SOS genes are rapidly induced while translesion synthesis polymerase activity is temporally regulated.Frontiers in microbiology · 2024Article
- Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The XP-D/DinG family of DNA helicases contributes to genomic stability in all three domains of life. Here, we investigate the role of one of these proteins, YoaA, of Escherichia coli. In E. coli, YoaA aids in tolerance to the nucleoside azidothymidine (AZT), a DNA replication inhibitor, and physically interacts with a subunit of the DNA polymerase III holoenzyme, HolC. We map the residues of YoaA required for HolC interaction to its C terminus by yeast two-hybrid analysis. We propose that this interaction competes with HolC's interaction with HolD and the rest of the replisome; YoaA indeed inhibits growth when overexpressed, dependent on this interaction region. By gene fusions, we show that YoaA is repressed by LexA and induced in response to DNA damage as part of the SOS response. Induction of YoaA by AZT is biphasic, with an immediate response after treatment and a slower response that peaks in the late log phase of growth. This growth-phase-dependent induction by AZT is not blocked by
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Registered trials
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