期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 106, 期 6, 页码 1748-1753出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0807193106
关键词
1D diffusion; ATPase; helicase; single molecule; motor protein
资金
- Deutsche Forschungsgemeinschaft
- Wellcome Trust [067439, 084086]
- Biotechnology and Biological Sciences Research Council
- Marie Curie Research Training Network DNA Enzymes''
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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