The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding

Jun Yong Ha, Hye Kyong Kim, Do Jin Kim, Kyoung Hoon Kim, Sung Jin Oh, Hyung Ho Lee, Hye Jin Yoon, Hyun Kyu Song, Se Won Suh

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


RecA plays a central role in the nonmutagenic repair of stalled replication forks in bacteria. RdgC, a recombination-associated DNA-binding protein, is a potential negative regulator of RecA function. Here, we have determined the crystal structure of RdgC from Pseudomonas aeruginosa. The J-shaped monomer has a unique fold and can be divided into three structural domains: Tip domain, center domain and base domain. Two such monomers dimerize to form a ring-shaped molecule of approximate 2-fold symmetry. Of the two inter-subunit interfaces within the dimer, one interface ('interface A') between tip/center domains is more nonpolar than the other ('interface B') between base domains. The structure allows us to propose that the RdgC dimer binds dsDNA through the central hole of ∼30° diameter. The proposed model is supported by our DNA-binding assays coupled with mutagenesis, which indicate that the conserved positively charged residues on the protein surface around the central hole play important roles in DNA binding. The novel ring-shaped architecture of the RdgC dimer has significant implications for its role in homologous recombination.

Original languageEnglish
Pages (from-to)2671-2681
Number of pages11
JournalNucleic acids research
Issue number8
Publication statusPublished - 2007 Apr

ASJC Scopus subject areas

  • Genetics


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