ArticleNucleic acids research2010
The RdgC protein employs a novel mechanism involving a finger domain to bind to circular DNA.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Lambdoid phages with abundant Chi recombination hotspots reflect diverse viral strategies for recombination-dependent growth.Genome research · 2025Article
- The crystal structure of bacteriophage λ RexA provides novel insights into the DNA binding properties of Rex-like phage exclusion proteins.Nucleic acids research · 2024Article
- DNA Packaging and Genomics of theJournal of virology · 2019Article
- Does DNA replication direct locus-specific recombination during host immune evasion by antigenic variation in the African trypanosome?Current genetics · 2017Review
- Proteomic Analysis of a Global Regulator GacS Sensor Kinase in the Rhizobacterium, Pseudomonas chlororaphis O6.The plant pathology journal · 2014Article
- Double-strand DNA end-binding and sliding of the toroidal CRISPR-associated protein Csn2.Nucleic acids research · 2013Article
- The Escherichia coli DinD protein modulates RecA activity by inhibiting postsynaptic RecA filaments.The Journal of biological chemistry · 2011Article
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4 authors.
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Abstract
The DNA-binding protein RdgC has been identified as an inhibitor of RecA-mediated homologous recombination in Escherichia coli. In Neisseria species, RdgC also has a role in virulence-associated antigenic variation. We have previously solved the crystal structure of the E. coli RdgC protein and shown it to form a toroidal dimer. In this study, we have conducted a mutational analysis of residues proposed to mediate interactions at the dimer interfaces. We demonstrate that destabilizing either interface has a serious effect on in vivo function, even though a stable complex with circular DNA was still observed. We conclude that tight binding is required for inhibition of RecA activity. We also investigated the role of the RdgC finger domain, and demonstrate that it plays a crucial role in the binding of circular DNA. Together, these data allow us to propose a model for how RdgC loads onto DNA. We discuss how RdgC might inhibit RecA-mediated strand exchange, and how RdgC might be displaced by other DNA metabolism enzymes such as polymerases and helicases.
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