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. 1984 May;81(9):2757-61.
doi: 10.1073/pnas.81.9.2757.

Mechanism of the concerted action of recA protein and helix-destabilizing proteins in homologous recombination

K Muniyappa, S L Shaner, S S Tsang, C M Radding

Mechanism of the concerted action of recA protein and helix-destabilizing proteins in homologous recombination

K Muniyappa et al. Proc Natl Acad Sci U S A. 1984 May.

Abstract

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.

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