Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 98, Issue 6, Pages 3045-3049Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.061029098
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Funding
- NIGMS NIH HHS [GM54215, R01 GM031657, GM31819, R37 GM031657, R01 GM031819, GM31657, R01 GM054215] Funding Source: Medline
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Type II DNA topoisomerases actively reduce the fractions of knotted and catenated circular DNA below thermodynamic equilibrium values. To explain this surprising finding, we designed a model in which topoisomerases introduce a sharp bend in DNA. Because the enzymes have a specific orientation relative to the bend, they act like Maxwell's demon, providing unidirectional strand passage. Quantitative analysis of the model by computer simulations proved that it can explain much of the experimental data. The required sharp DNA bend was demonstrated by a greatly increased cyclization of short DNA fragments from topoisomerase binding and by direct visualization with electron microscopy.
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