Mechanism of the concerted action of recA protein and helix-destabilizing proteins in homologous recombination.
Secondary structure in single-stranded DNA impedes the presynaptic association of recA protein and consequently blocks the formation of joint molecules as evidenced by effects of temperature, nucleotide sequence, and ionic conditions. Escherichia coli single-strand-binding protein eliminates sequence-specific "cold spots" by removing folds even from sites of strong secondary structure. Thus, destabilization of secondary structure in single-stranded DNA is critical for the action of recA protein, whereas specific interactions directly between helix-destabilizing proteins and recA protein are unimportant.
D001483:Base Sequence; D004265:DNA Helicases / Q000235:genetics*; D004277:DNA, Single-Stranded / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics*; D008274:Magnesium / Q000502:physiology; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011938:Rec A Recombinases / Q000235:genetics*; D011995:Recombination, Genetic; D013696:Temperature; D014764:Viral Proteins
D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D014764:Viral Proteins; C060035:gp32 protein, Enterobacteria phage T4; C027729:helix-destabilizing proteins; D011938:Rec A Recombinases; D004265:DNA Helicases; D008274:Magnesium