Asymmetric activation of Xer site-specific recombination by FtsK.
Chromosome dimers, which frequently form in Escherichia coli, are resolved by the combined action of two tyrosine recombinases, XerC and XerD, acting at a specific site on the chromosome, dif, together with the cell division protein FtsK. The C-terminal domain of FtsK (FtsK(C)) is a DNA translocase implicated in helping synapsis of the dif sites and in locally promoting XerD strand exchanges after synapse formation. Here we show that FtsK(C) ATPase activity is directly involved in the local activation of Xer recombination at dif, by using an intermolecular recombination assay that prevents significant DNA translocation, and we confirm that FtsK acts before Holliday junction formation. We show that activation only occurs with a DNA segment adjacent to the XerD-binding site of dif. Only one such DNA extension is required. Taken together, our data suggest that FtsK needs to contact the XerD recombinase to switch its activity on using ATP hydrolysis.
Massey
Thomas H
TH
Division of Molecular Genetics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Aussel
Laurent
L
Barre
François-Xavier
FX
Sherratt
David J
DJ
D004247:DNA / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology; D029968:Escherichia coli Proteins / Q000378:metabolism*; D019426:Integrases / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011995:Recombination, Genetic / Q000502:physiology*
D029968:Escherichia coli Proteins; C096452:FtsK protein, E coli; D008565:Membrane Proteins; C473360:XerC protein, E coli; D004247:DNA; D019426:Integrases; C473361:XerD protein, E coli