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  • Title: Homologous DNA pairing promoted by a 20-amino acid peptide derived from RecA.
    Author: Voloshin ON, Wang L, Camerini-Otero RD.
    Journal: Science; 1996 May 10; 272(5263):868-72. PubMed ID: 8629021.
    Abstract:
    The molecular structure of the Escherichia coli RecA protein in the absence of DNA revealed two disordered or mobile loops that were proposed to be DNA binding sites. A short peptide spanning one of these loops was shown to carry out the key reaction mediated by the whole RecA protein: pairing (targeting) of a single-stranded DNA to its homologous site on a duplex DNA. In the course of the reaction the peptide bound to both substrate DNAs, unstacked the single-stranded DNA, and assumed a beta structure. These events probably recapitulate the underlying molecular pathway or mechanism used by homologous recombination proteins.
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