Functional significance of octameric RuvA for a branch migration complex from Thermus thermophilus.
The RuvAB complex promotes migration of Holliday junction at the late stage of homologous recombination. The RuvA tetramer specifically recognizes Holliday junction to form two types of complexes. A single tetramer is bound to the open configuration of the junction DNA in complex I, while the octameric RuvA core structure sandwiches the same junction in complex II. The hexameric RuvB rings, symmetrically bound to both sides of RuvA on Holliday junction, pump out DNA duplexes, depending upon ATP hydrolysis. We investigated functional differences between the wild-type RuvA from Thermus thermophilus and mutants impaired the ability of complex II formation. These mutant RuvA, exclusively forming complex I, reduced activities of branch migration and ATP hydrolysis, suggesting that the octameric RuvA is essential for efficient branch migration. Together with our recent electron microscopic analysis, this finding provides important insights into functional roles of complex II in the coordinated branch migration mechanism.
Fujiwara
Yoshie
Y
Graduate School of Engineering Science, Osaka University, 1-3, Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Mayanagi
Kouta
K
Morikawa
Kosuke
K
D004265:DNA Helicases / Q000235:genetics / Q000378:metabolism*; D045566:DNA, Cruciform / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D011995:Recombination, Genetic / Q000502:physiology*; D016963:Thermus thermophilus / Q000378:metabolism*
D045566:DNA, Cruciform; D029968:Escherichia coli Proteins; C071059:Holliday junction DNA helicase, E coli; D004265:DNA Helicases