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| Subject Categories: Structural Biology | Genome Stability & Dynamics |
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| The EMBO Journal
(2004) 23, 2029–2038, doi:10.1038/sj.emboj.7600222 Published online 29 April 2004 |
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| Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair |
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| Byung Il Lee1, Kyoung Hoon Kim1, Soo Jeong Park2, Soo Hyun Eom2, Hyun Kyu Song3 and Se Won Suh1 |
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1 Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul, Korea 2 Department of Life Science, Kwangju Institute of Science and Technology, Kwangju, Korea 3 Research Institute, National Cancer Center, Goyang, Gyeonggi, Korea To whom correspondence should be addressed Se Won Suh, Department of Chemistry, School of Chemistry & Molecular Engineering, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea. Tel.: +82 2 880 6653; Fax: +82 2 889 1568; E-mail: sewonsuh@snu.ac.kr Received 18 December 2003; Accepted 6 April 2004; Published online 29 April 2004. |
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| Abstract |
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| RecR, together with RecF and RecO, facilitates RecA loading in the RecF pathway of homologous recombinational DNA repair in procaryotes . The human Rad52 protein is a functional counterpart of RecFOR. We present here the crystal structure of RecR from Deinococcus radiodurans (DR RecR). A monomer of DR RecR has a two-domain structure: the N-terminal domain with a helix–hairpin–helix (HhH) motif and the C-terminal domain with a Cys4 zinc-finger motif, a Toprim domain and a Walker B motif. Four such monomers form a ring-shaped tetramer of 222 symmetry with a central hole of 30-35 Å diameter. In the crystal, two tetramers are concatenated, implying that the RecR tetramer is capable of opening and closing. We also show that DR RecR binds to both dsDNA and ssDNA, and that its HhH motif is essential for DNA binding. |
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| Keywords: DNA clamp, DNA repair, homologous recombination, RecF pathway, RecR |
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Top of page MORE ARTICLES LIKE THISThese links to content published by NPG are automatically generated NEWS AND VIEWSGenetic recombination From competition to collaboration Nature News and Views (22 Jan 1998) RESEARCHCrystal structure and DNA-binding analysis of RecO from Deinococcus radiodurans The EMBO Journal Article (09 Mar 2005) Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding The EMBO Journal Article Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding The EMBO Journal Article (11 Jul 2007) |
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