Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 20, Pages 9123-9128Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1001637107
Keywords
diffusion; helicase; motor; switch
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Funding
- Deutsche Forschungsgemeinschaft
- EU [MRTN-CT-2005-019566]
- Wellcome Trust [084086]
- Dresden International Graduate School for Biomedicine and Bioengineering, DFG (German Research Foundation)
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Cleavage of viral DNA by the bacterial Type III Restriction-Modification enzymes requires the ATP-dependent long-range communication between a distant pair of DNA recognition sequences. The classical view is that Type III endonuclease activity is only activated by a pair of asymmetric sites in a specific head-to-head inverted repeat. Based on this assumption and due to the presence of helicase domains in Type III enzymes, various motor-driven DNA translocation models for communication have been suggested. Using both single-molecule and ensemble assays we demonstrate that Type III enzymes can also cleave DNA with sites in tail-to-tail repeat with high efficiency. The ability to distinguish both inverted repeat substrates from direct repeat substrates in a manner independent of DNA topology or accessory proteins can only be reconciled with an alternative sliding mode of communication.
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