Nature Structural & Molecular Biology
- 13, 965 - 972 (2006)
Published online: 22 October 2006; | doi:10.1038/nsmb1158
The FtsK  domain directs oriented DNA translocation by interacting with KOPSViknesh Sivanathan1, 4, Mark D Allen2, 4, Charissa de Bekker1, Rachel Baker1, Lidia K Arciszewska1, Stefan M Freund2, Mark Bycroft2, Jan Löwe3 & David J Sherratt11
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK. 2
Centre for Protein Engineering, Medical Research Council, Hills Road, Cambridge CB2 2QH, UK. 3
Laboratory of Molecular Biology, Medical Research Council, Hills Road, Cambridge CB2 2QH, UK. 4
These authors contributed equally to this work.
Correspondence should be addressed to David J Sherratt sherratt@bioch.ox.ac.uk The bacterial septum-located DNA translocase FtsK coordinates circular chromosome segregation with cell division. Rapid translocation of DNA by FtsK is directed by 8-base-pair DNA motifs (KOPS), so that newly replicated termini are brought together at the developing septum, thereby facilitating completion of chromosome segregation. Translocase functions reside in three domains,  ,  and  . FtsK are necessary and sufficient for ATP hydrolysis–dependent DNA translocation, which is modulated by FtsK through its interaction with KOPS. By solving the FtsK structure by NMR, we show that is a winged-helix domain. NMR chemical shift mapping localizes the DNA-binding site on the domain. Mutated proteins with substitutions in the FtsK DNA-recognition helix are impaired in DNA binding and KOPS recognition, yet remain competent in DNA translocation and XerCD-dif site-specific recombination, which facilitates the late stages of chromosome segregation.
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