title: Simple topology: FtsK-directed recombination at the dif site.
abstract: FtsK is a multifunctional protein, which, in Escherichia coli, co-ordinates the essential functions of cell division, DNA unlinking and chromosome segregation. Its C-terminus is a DNA translocase, the fastest yet characterized, which acts as a septum-localized DNA pump. FtsK's C-terminus also interacts with the XerCD site-specific recombinases which act at the dif site, located in the terminus region. The motor domain of FtsK is an active translocase in vitro, and, when incubated with XerCD and a supercoiled plasmid containing two dif sites, recombination occurs to give unlinked circular products. Despite years of research the mechanism for this novel form of topological filter remains unknown.
authors.affiliation: School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW 2308, Australia. Ian.Grainge@newcastle.edu.au
authors.forename: Ian
authors.initials: I
authors.lastname: Grainge
mesh_terms: D004254:DNA Nucleotidyltransferases; D004269:DNA, Bacterial / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D011995:Recombination, Genetic
chemical_list: D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; C096452:FtsK protein, E coli; D008565:Membrane Proteins; D004254:DNA Nucleotidyltransferases; C077570:Site-specific recombinase