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PMID:18722176

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Citation

Löwe, J, Ellonen, A, Allen, MD, Atkinson, C, Sherratt, DJ and Grainge, I (2008) Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol. Cell 31:498-509

Abstract

Dimeric circular chromosomes, formed by recombination between monomer sisters, cannot be segregated to daughter cells at cell division. XerCD site-specific recombination at the Escherichia coli dif site converts these dimers to monomers in a reaction that requires the DNA translocase FtsK. Short DNA sequences, KOPS (GGGNAGGG), which are polarized toward dif in the chromosome, direct FtsK translocation. FtsK interacts with KOPS through a C-terminal winged helix domain gamma. The crystal structure of three FtsKgamma domains bound to 8 bp KOPS DNA demonstrates how three gamma domains recognize KOPS. Using covalently linked dimers of FtsK, we infer that three gamma domains per hexamer are sufficient to recognize KOPS and load FtsK and subsequently activate recombination at dif. During translocation, FtsK fails to recognize an inverted KOPS sequence. Therefore, we propose that KOPS act solely as a loading site for FtsK, resulting in a unidirectionally oriented hexameric motor upon DNA.

Links

PubMed PMC2570039 Online version:10.1016/j.molcel.2008.05.027

Keywords

Adenosine Triphosphate/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Biological Assay; Crystallography, X-Ray; DNA, Bacterial/metabolism; Dimerization; Hydrolysis; Models, Biological; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Transport; Pseudomonas aeruginosa/metabolism; Recombination, Genetic

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:FTSK

enables

GO:0003677: DNA binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ECOLI:FTSK

enables

GO:0016887: ATPase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

See also

References

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