ArticlePLoS genetics2015
A RecA protein surface required for activation of DNA polymerase V.
Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Acinetobacter baumannii encodes multiple mutagenically and biochemically active DNA polymerase V variants.Nucleic acids research · 2026Article
- Common themes in architecture and interactions of prokaryotic PolB2 and Pol V mutasomes inferred fromComputational and structural biotechnology journal · 2025Article
- Pathogen-encoded Rum DNA polymerase drives rapid bacterial drug resistance.Nucleic acids research · 2024Article
- Age of Antibiotic Resistance in MDR/XDR Clinical Pathogen ofPharmaceuticals (Basel, Switzerland) · 2023Review
- Investigating the composition and recruitment of the mycobacterial ImuA'-ImuB-DnaE2 mutasome.eLife · 2023Article
- Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023Review
- Genetic Factors Affect the Survival and Behaviors of Selected Bacteria during Antimicrobial Blue Light Treatment.International journal of molecular sciences · 2021Review
- RecA-independent recombination: Dependence on the Escherichia coli RarA protein.Molecular microbiology · 2021Article
- Article
- Targeting evolution of antibiotic resistance by SOS response inhibition.Computational and structural biotechnology journal · 2021Review
- A Comprehensive View of Translesion Synthesis in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2020Review
- Role of RNase H enzymes in maintaining genome stability in Escherichia coli expressing a steric-gate mutant of pol VDNA repair · 2019Article
- New insights into the structures and interactions of bacterial Y-family DNA polymerases.Nucleic acids research · 2019Article
- The SOS system: A complex and tightly regulated response to DNA damage.Environmental and molecular mutagenesis · 2019Review
- RecFOR epistasis group: RecF and RecO have distinct localizations and functions in Escherichia coli.Nucleic acids research · 2019Article
- Conformational regulation of Escherichia coli DNA polymerase V by RecA and ATP.PLoS genetics · 2019Article
- SetRDNA repair · 2019Article
- The DnaE polymerase from Deinococcus radiodurans features RecA-dependent DNA polymerase activity.Bioscience reports · 2016Article
- RecA stimulates AlkB-mediated direct repair of DNA adducts.Nucleic acids research · 2016Article
- Insights into the complex levels of regulation imposed on Escherichia coli DNA polymerase V.DNA repair · 2016Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
DNA polymerase V (pol V) of Escherichia coli is a translesion DNA polymerase responsible for most of the mutagenesis observed during the SOS response. Pol V is activated by transfer of a RecA subunit from the 3'-proximal end of a RecA nucleoprotein filament to form a functional complex called DNA polymerase V Mutasome (pol V Mut). We identify a RecA surface, defined by residues 112-117, that either directly interacts with or is in very close proximity to amino acid residues on two distinct surfaces of the UmuC subunit of pol V. One of these surfaces is uniquely prominent in the active pol V Mut. Several conformational states are populated in the inactive and active complexes of RecA with pol V. The RecA D112R and RecA D112R N113R double mutant proteins exhibit successively reduced capacity for pol V activation. The double mutant RecA is specifically defective in the ATP binding step of the activation pathway. Unlike the classic non-mutable RecA S117F (recA1730), the RecA D112R N113R variant exhibits no defect in filament formation on DNA and promotes all other RecA activities efficiently. An important pol V activation surface of RecA protein is thus centered in a region encompassing amino acid residues 112, 113, and 117, a surface exposed at the 3'-proximal end of a RecA filament. The same RecA surface is not utilized in the RecA activation of the homologous and highly mutagenic RumA'2B polymerase encoded by the integrating-conjugative element (ICE) R391, indicating a lack of structural conservation between the two systems. The RecA D112R N113R protein represents a new separation of function mutant, proficient in all RecA functions except SOS mutagenesis.
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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.