Article
- The EMBO Journal (2007) 26, 867 - 877
- doi:10.1038/sj.emboj.7601537
Published online: 25 January 2007
Subject Category:
Structural conservation of RecF and Rad50: implications for DNA recognition and RecF function
Olga Koroleva1, Nodar Makharashvili1, Charmain T Courcelle2, Justin Courcelle2 and Sergey Korolev1
- Edward A Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St Louis, MO, USA
- Department of Biology, Portland State University, Portland, OR, USA
Correspondence to:
Sergey Korolev, Department of Biochemistry and Molecular Biology, St Louis University School of Medicine, 1402 South Grand Blvd, St Louis, MO 63104, USA. Tel.: +1 314 977 9261; Fax: +1 314 977 9205; E-mail: korolevs@slu.edu
Received 10 July 2006; Accepted 8 December 2006
Abstract
RecF, together with RecO and RecR, belongs to a ubiquitous group of recombination mediators (RMs) that includes eukaryotic proteins such as Rad52 and BRCA2. RMs help maintain genome stability in the presence of DNA damage by loading RecA-like recombinases and displacing single-stranded DNA-binding proteins. Here, we present the crystal structure of RecF from Deinococcus radiodurans. RecF exhibits a high degree of structural similarity with the head domain of Rad50, but lacks its long coiled-coil region. The structural homology between RecF and Rad50 is extensive, encompassing the ATPase subdomain and the so-called 'Lobe II' subdomain of Rad50. The pronounced structural conservation between bacterial RecF and evolutionarily diverged eukaryotic Rad50 implies a conserved mechanism of DNA binding and recognition of the boundaries of double-stranded DNA regions. The RecF structure, mutagenesis of conserved motifs and ATP-dependent dimerization of RecF are discussed with respect to its role in promoting presynaptic complex formation at DNA damage sites.
Keywords:
- DNA binding,
- Rad50,
- RecF,
- recombination,
- structure
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