Structural conservation of RecF and Rad50: implications for DNA recognition and RecF function.
EMBO J
; 26(3): 867-77, 2007 Feb 07.
Article
em En
| MEDLINE
| ID: mdl-17255941
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
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Modelos Moleculares
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Evolução Molecular
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Deinococcus
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Proteínas de Ligação a DNA
Idioma:
En
Ano de publicação:
2007
Tipo de documento:
Article