Nucleic Acids Research, Vol 26, Issue 7 1560-1566, Copyright © 1998 by Oxford University Press
SN Chan, SD Vincent and RG Lloyd
Homologous recombination is a fundamental cellular process that shapes and
reshapes the genomes of all organisms and promotes repair of damaged DNA. A
key step in this process is the resolution of Holliday junctions formed by
homologous DNA pairing and strand exchange. In Escherichia coli , a
Holliday junction is processed into recombinant products by the concerted
activities of the RuvA and RuvB proteins, which together drive branch
migration, and RuvC endonuclease, which resolves the structure. In the
absence of RuvABC, recombination can be promoted by increasing the
expression of the RusA endonuclease, a Holliday junction resolvase encoded
by a cryptic prophage gene. Here, we describe the DNA binding properties of
RusA. We found that RusA was highly selective for branched molecules and
formed complexes with these structures even in the presence of a large
excess of linear duplex DNA. However, it does bind weakly to linear duplex
DNA. Under conditions where there was no detectable binding to duplex DNA,
RusA formed a highly structured complex with a synthetic Holliday junction
that was remarkably stable and insensitive to divalent metal ions. The
duplex arms were found to adopt a specific alignment within this complex
that approximated to a tetrahedral conformation of the junction.
ARTICLES
Recognition and manipulation of branched DNA by the RusA Holliday junction resolvase of Escherichia coli
Department of Genetics, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, UK.
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