Abstract
To cleave DNA, the Type III RM (restriction-modification) enzymes must communicate the relative orientation of two recognition sequences, which may be separated by many thousands of base pairs. This long-range interaction requires ATP hydrolysis by a helicase domain, and both active (DNA translocation) and passive (DNA sliding) modes of motion along DNA have been proposed. Potential roles for ATP binding and hydrolysis by the helicase domains are discussed, with a focus on bipartite ATPases that act as molecular switches.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphate / pharmacology*
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Animals
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Binding Sites / drug effects
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Binding Sites / genetics
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DNA / chemistry
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DNA / metabolism*
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Deoxyribonucleases, Type III Site-Specific / metabolism*
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Deoxyribonucleases, Type III Site-Specific / physiology*
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Humans
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Models, Biological
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Movement / physiology*
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Nucleic Acid Conformation / drug effects
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Protein Binding / drug effects
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Protein Binding / physiology
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Protein Transport
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Substrate Specificity
Substances
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Adenosine Triphosphate
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DNA
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Deoxyribonucleases, Type III Site-Specific