Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 14, Pages 4292-4297Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1416746112
Keywords
helicase; RecQ; mechanism; aromatic-rich loop; DNA bending
Categories
Funding
- National Institutes of Health (NIH) Grant [GM098885]
- NIH Training Grant in Molecular Biosciences [GM07215]
- NIH Grant [S10RR027000, P41GM103399]
- US DOE [DE-AC02-06CH11357]
- Michigan Economic Development Corporation [085P1000817]
- Michigan Technology Tri-Corridor
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RecQ helicases unwind remarkably diverse DNA structures as key components of many cellular processes. How RecQ enzymes accommodate different substrates in a unified mechanism that couples ATP hydrolysis to DNA unwinding is unknown. Here, the X-ray crystal structure of the Cronobacter sakazakii RecQ catalytic core domain bound to duplex DNA with a 3' single-stranded extension identifies two DNA-dependent conformational rearrangements: a winged-helix domain pivots similar to 90 degrees to close onto duplex DNA, and a conserved aromatic-rich loop is remodeled to bind ssDNA. These changes coincide with a restructuring of the RecQ ATPase active site that positions catalytic residues for ATP hydrolysis. Complex formation also induces a tight bend in the DNA and melts a portion of the duplex. This bending, coupled with translocation, could provide RecQ with a mechanism for unwinding duplex and other DNA structures.
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