Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 6, Pages 1748-1753Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0807193106
Keywords
1D diffusion; ATPase; helicase; single molecule; motor protein
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Funding
- Deutsche Forschungsgemeinschaft
- Wellcome Trust [067439, 084086]
- Biotechnology and Biological Sciences Research Council
- Marie Curie Research Training Network DNA Enzymes''
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To cleave DNA, Type III restriction enzymes must communicate the relative orientation of two asymmetric recognition sites over hundreds of base pairs. The basis of this long-distance communication, for which ATP hydrolysis by their helicase domains is required, is poorly understood. Several conflicting DNA-looping mechanisms have been proposed, driven either by active DNA translocation or passive 3D diffusion. Using single-molecule DNA stretching in combination with bulk-solution assays, we provide evidence that looping is both highly unlikely and unnecessary, and that communication is strictly confined to a 1D route. Integrating our results with previous data, a simple communication scheme is concluded based on 1D diffusion along DNA.
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