ArticleJournal of bacteriology2013
A single residue unique to DinB-like proteins limits formation of the polymerase IV multiprotein complex in Escherichia coli.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Combining Electrochemical Reduction with Biosynthesis for Directed Conversion of COAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- A new component of the DNA damage response biofilm axis in Acinetobacter baumannii is a TetR-like DNA damage response regulator.FEMS microbiology letters · 2026Article
- Identification of EppR, a Second Repressor of Error-Prone DNA Polymerase Genes in Acinetobacter baumannii.Molecular microbiology · 2025Article
- Replication stalling activates SSB for recruitment of DNA damage tolerance factors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A gatekeeping function of the replicative polymerase controls pathway choice in the resolution of lesion-stalled replisomes.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Slow extension of the invading DNA strand in a D-loop formed by RecA-mediated homologous recombination may enhance recognition of DNA homology.The Journal of biological chemistry · 2019Article
- Residues in the fingers domain of the translesion DNA polymerase DinB enable its unique participation in error-prone double-strand break repair.The Journal of biological chemistry · 2019Article
- The positioning of Chi sites allows the RecBCD pathway to suppress some genomic rearrangements.Nucleic acids research · 2019Article
- Single-molecule imaging reveals multiple pathways for the recruitment of translesion polymerases after DNA damage.Nature communications · 2017Article
- RNA Primer Extension Hinders DNA Synthesis byFrontiers in microbiology · 2017Article
- A Genetic Selection for dinB Mutants Reveals an Interaction between DNA Polymerase IV and the Replicative Polymerase That Is Required for Translesion Synthesis.PLoS genetics · 2015Article
- Recombinase and translesion DNA polymerase decrease the speed of replication fork progression during the DNA damage response in Escherichia coli cells.Nucleic acids research · 2015Article
- Selection of dinB alleles suppressing survival loss upon dinB overexpression in Escherichia coli.Journal of bacteriology · 2014Article
- DNA polymerase IV mediates efficient and quick recovery of replication forks stalled at N2-dG adducts.Nucleic acids research · 2014Article
- A ΔdinB mutation that sensitizes Escherichia coli to the lethal effects of UV- and X-radiation.Mutation researchArticle
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The activity of DinB is governed by the formation of a multiprotein complex (MPC) with RecA and UmuD. We identified two highly conserved surface residues in DinB, cysteine 66 (C66) and proline 67 (P67). Mapping on the DinB tertiary structure suggests these are noncatalytic, and multiple-sequence alignments indicate that they are unique among DinB-like proteins. To investigate the role of the C66-containing surface in MPC formation, we constructed the dinB(C66A) derivative. We found that DinB(C66A) copurifies with its interacting partners, RecA and UmuD, to a greater extent than DinB. Notably, copurification of RecA with DinB is somewhat enhanced in the absence of UmuD and is further increased for DinB(C66A). In vitro pulldown assays also indicate that DinB(C66A) binds RecA and UmuD better than DinB. We note that the increased affinity of DinB(C66A) for UmuD is RecA dependent. Thus, the C66-containing binding surface appears to be critical to modulate interaction with UmuD, and particularly with RecA. Expression of dinB(C66A) from the chromosome resulted in detectable differences in dinB-dependent lesion bypass fidelity and homologous recombination. Study of this DinB derivative has revealed a key surface on DinB, which appears to modulate the strength of MPC binding, and has suggested a binding order of RecA and UmuD to DinB. These findings will ultimately permit the manipulation of these enzymes to deter bacterial antibiotic resistance acquisition and to gain insights into cancer development in humans.
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