Nucleic Acids Research, Vol 27, Issue 15 3049-3056, Copyright © 1999 by Oxford University Press
P McGlynn and RG Lloyd
The RecG helicase of Escherichia coli is necessary for efficient
recombination and repair of DNA in vivo and has been shown to catalyse the
unwinding of DNA junctions in vitro. Despite these findings, the precise
role of RecG remains elusive. However, models have been proposed in which
RecG promotes the resolution of linked duplexes by targeting three-strand
junctions present at D-loops. One such model postulates that RecG catalyses
the formation of four-strand (Holliday) junctions from three-strand
junctions. To test this model, the DNA binding and unwinding activities of
RecG were analysed using synthetic three- and four-strand junctions. The
substrate specificity of RecG was found to depend critically on the
concentrations of ATP and MgCl(2)and under certain conditions RecG
preferentially unwound three-strand junction DNA. This was at least partly
due to the larger inhibitory effect of MgCl(2)on the binding of four-strand
as opposed to three- strand junctions by RecG. Thus RecG may be targeted to
three-strand junctions in vivo whilst still being able to branch migrate
the four- strand junctions formed as a result of the initial helicase
reaction. The increase in the dissociation constant of RecG on conversion
of a three-strand into a four-strand junction may also facilitate
resolution of the four-strand junction by the RuvABC complex.
ARTICLES
RecG helicase activity at three- and four-strand DNA structures
Institute of Genetics, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK.
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