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

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...

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Bibliographic Details
Published in:Genes & development 1999-08, Vol.13 (15), p.2005-2016
Main Authors: Mazin, A V, Kowalczykowski, S C
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - analogs & derivatives
Adenosine Triphosphate - metabolism
Base Pairing
Base Sequence
Binding, Competitive
DNA - genetics
DNA - metabolism
DNA, Single-Stranded - genetics
DNA, Single-Stranded - metabolism
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Kinetics
Models, Genetic
Mutation
Nucleic Acid Heteroduplexes - genetics
Nucleic Acid Hybridization
Protein Binding
Rec A Recombinases - genetics
Rec A Recombinases - metabolism
Recombination, Genetic - genetics
Research Paper
Sequence Homology, Nucleic Acid
Temperature
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Summary: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.
ISSN:0890-9369
DOI:10.1101/gad.13.15.2005