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RecF Recognizes DNA Damage in Concert with RecR
Author(s) -
Makharashvili Nodar,
Koroleva Olga,
Korolev Sergey
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.989.7
Subject(s) - dna , biophysics , recombinase , recombination , dna damage , biology , protein–dna interaction , atp hydrolysis , microbiology and biotechnology , chemistry , dna binding protein , genetics , biochemistry , gene , enzyme , transcription factor , atpase
The RecFOR recombination mediator complex detects single‐stranded gapped DNA and recruits RecA recombinase at the damage site through an unknown mechanism. Our structural and biochemical studies suggest that an interaction between a symmetric RecF dimer and an asymmetric broken DNA structure initiates recruitment of RecR and ‐O proteins to the site. We demonstrate that an ATP‐dependent dimerization of RecF is essential for its other activities, DNA binding and interaction with RecR. In the presence of ATP, RecF alone binds DNA relatively weakly. No preferential binding towards single stranded (ss)/double stranded (ds) DNA junctions was observed, while there was a slight preference for ssDNA. RecR drastically changes RecF's interaction with DNA. It substantially increases RecF's affinity towards dsDNA while affinity to ssDNA remains the same. RecR also alters RecF‐mediated ATP hydrolysis; the rate increases in the presence of ssDNA, while it decreases in the presence of dsDNA. Our findings suggest a dynamic multi‐step mechanism of damage site recognition by the RecFR complex as the first step in the recombination mediation reaction.