Mechanism of topology simplification by type II DNA topoisomerases.
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.
Department of Chemistry, New York University, Washington Square, New York, NY 10003, USA. alex.vologodskii@nyu.edu
A V
AV
Vologodskii
W
W
Zhang
V V
VV
Rybenkov
A A
AA
Podtelezhnikov
D
D
Subramanian
J D
JD
Griffith
N R
NR
Cozzarelli
D003198:Computer Simulation; D004250:DNA Topoisomerases, Type II / Q000378:metabolism* / Q000648:ultrastructure; D004270:DNA, Circular / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D008854:Microscopy, Electron; D008958:Models, Molecular
D004270:DNA, Circular; D004250:DNA Topoisomerases, Type II