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Homologous DNA Pairing Promoted by a 20-Amino Acid Peptide Derived from RecA
Oleg N. Voloshin, Lijiang Wang and R. Daniel Camerini-Otero
New Series, Vol. 272, No. 5263 (May 10, 1996), pp. 868-872
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/2890215
Page Count: 5
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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 β structure. These events probably recapitulate the underlying molecular pathway or mechanism used by homologous recombination proteins.
Science © 1996 American Association for the Advancement of Science