3D Tissue Models

Molecular Mechanism of Sequence-Directed DNA Loading and Translocation by FtsK

TypeWhite Paper Summary

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 γ. The crystal structure of three FtsKγ domains bound to 8 bp KOPS DNA demonstrates how three γ domains recognize KOPS. Using covalently linked dimers of FtsK, we infer that three γ 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.

Name:Dr. Edward Seto
Name:Mark D. Allen
Name:David J. Sherratt
Name:Richard A. Young
Name:Xiang-Jiao Yang
Name:Silvestro G Conticello
Name:Karuna Ganesh
Name:Noriko Shimazaki
Name:Prafulla Raval
Name:Go Watanabe
Name:Michael R Lieber
Name:Jan Löwe
Name:Ian Grainge
Name:Antti Ellonen
Name:Claire Atkinson
Name:Michael R Stallcup
Name:Nuria Lopez Bigas
Name:Elizaveta V Benevolenskaya
Name:Tomasz A Kisiel
Name:Sumeet Gupta
Name:Heather L Murray
Name:Robert Roeder
Organization:Rockefeller University

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