A novel property of the RecA nucleoprotein filament: Activation of double-stranded DNA for strand exchange in trans

Alexander V. Mazin, Stephen C. Kowalczykowski

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

RecA protein catalyzes DNA strand exchange, a basic step of homologous recombination. Upon binding to single-stranded DNA (ssDNA), RecA protein forms a helical nucleoprotein filament. Normally, this nucleoprotein filament binds double-stranded DNA (dsDNA) and promotes exchange of base pairs between this dsDNA and the homologous ssDNA that is contained within this filament. Here, we demonstrate that this bound dsDNA can be activated by interaction with a heterologous RecA nucleoprotein filament for a novel type of strand exchange with homologous ssDNA that is external to, and, therefore, not within, the filament. We refer to this novel DNA strand exchange as being in trans. Thus, the RecA nucleoprotein filament is a protein scaffold that activates dsDNA for strand exchange with ssDNA either within the filament or external to it. This new property demonstrates that the RecA nucleoprotein filament makes dsDNA receptive for DNA strand exchange, and it defines an early step of the homology recognition mechanism.

Original languageEnglish (US)
Pages (from-to)2005-2016
Number of pages12
JournalGenes and Development
Volume13
Issue number15
StatePublished - Aug 1 1999

Keywords

  • Genetic recombination
  • Homology recognition
  • Protein-DNA interactions

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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