Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

Homologous DNA Pairing Promoted by a 20-Amino Acid Peptide Derived from RecA

Oleg N. Voloshin, Lijiang Wang and R. Daniel Camerini-Otero
Science
New Series, Vol. 272, No. 5263 (May 10, 1996), pp. 868-872
Stable URL: http://www.jstor.org/stable/2890215
Page Count: 5
  • More info
  • Cite this Item
Homologous DNA Pairing Promoted by a 20-Amino Acid Peptide Derived from RecA
Preview not available

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 β structure. These events probably recapitulate the underlying molecular pathway or mechanism used by homologous recombination proteins.

Page Thumbnails

  • Thumbnail: Page 
868
    868
  • Thumbnail: Page 
869
    869
  • Thumbnail: Page 
870
    870
  • Thumbnail: Page 
871
    871
  • Thumbnail: Page 
872
    872