All major regions of FtsK are required for resolution of chromosome dimers.
Resolution of chromosome dimers, by site-specific recombination between dif sites, is carried out in Escherichia coli by XerCD recombinase in association with the FtsK protein. We show here that a variety of altered FtsK polypeptides, consisting of the N-terminal (cell division) domain alone or with deletions in the proline-glutamine-rich part of the protein, or polypeptides consisting of the C-terminal domain alone are all unable to carry out dif recombination. Alteration of the putative nucleotide-binding site also abolishes the ability of FtsK to carry out recombination between dif sites.
Boyle
D S
DS
Institute of Cell & Molecular Biology, University of Edinburgh, Scotland. Dboyle@skcc.org
Grant
D
D
Draper
G C
GC
Donachie
W D
WD
D002876:Chromosomes, Bacterial; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D008565:Membrane Proteins / Q000378:metabolism*; D011995:Recombination, Genetic; D017384:Sequence Deletion
D029968:Escherichia coli Proteins; C096452:FtsK protein, E coli; D008565:Membrane Proteins