1997
DOI: 10.1126/science.277.5326.690
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Simplification of DNA Topology Below Equilibrium Values by Type II Topoisomerases

Abstract: Type II DNA topoisomerases catalyze the interconversion of DNA topoisomers by transporting one DNA segment through another. The steady-state fraction of knotted or catenated DNA molecules produced by prokaryotic and eukaryotic type II topoisomerases was found to be as much as 80 times lower than at thermodynamic equilibrium. These enzymes also yielded a tighter distribution of linking number topoisomers than at equilibrium. Thus, topoisomerases do not merely catalyze passage of randomly juxtaposed DNA segments… Show more

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Cited by 257 publications
(373 citation statements)
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“…Since the publication by Rybenkov et al (1997) demonstrating that Type IIA topoisomerases (with the exception of DNA gyrase) reduce the level of DNA linking, knotting, and supercoiling to below thermal equilibrium vales, it has remained a puzzle how these enzymes simplify global topology. Energetically, below-equilibrium topology simplification by Topo IIA does not violate thermodynamics since these topoisomerases utilize ATP as an energy source, so they can work against the thermal equilibrium limit.…”
Section: Dna Twist (Torsion)-dependent Protein Activitymentioning
confidence: 99%
See 1 more Smart Citation
“…Since the publication by Rybenkov et al (1997) demonstrating that Type IIA topoisomerases (with the exception of DNA gyrase) reduce the level of DNA linking, knotting, and supercoiling to below thermal equilibrium vales, it has remained a puzzle how these enzymes simplify global topology. Energetically, below-equilibrium topology simplification by Topo IIA does not violate thermodynamics since these topoisomerases utilize ATP as an energy source, so they can work against the thermal equilibrium limit.…”
Section: Dna Twist (Torsion)-dependent Protein Activitymentioning
confidence: 99%
“…Topo IA and IB, on the other hand, do not utilize external energy, so they can only achieve thermodynamic equilibrium topological distributions. It remains unclear, however, how Topo IIA employ some of the energy of ATP hydrolysis to distinguish DNA juxtapositions in catenanes and knots and writhe of supercoils, from those occurring within or between DNA molecules due to thermal fluctuations (Rybenkov et al 1997). This implies that Topo IIA must Bsense^which juxtapositions simplify global DNA topology when unlinked.…”
Section: Dna Twist (Torsion)-dependent Protein Activitymentioning
confidence: 99%
“…(1), (2), (14), (21). So far, it was (hopefully) clear from the context in every place which x we have in mind.…”
Section: B Winding Around a Disc (B > 0)mentioning
confidence: 99%
“…Moreover, apart from networks, there is now another large "consumer" for polymer topology, this is DNA physics. The DNA double helix is frequently found in a closed loop form, it forms knots of various kinds [19,20], and there are special enzymes spending energy to simplify the entanglements [21].…”
Section: Introductionmentioning
confidence: 99%
“…Mechanistically operating on writhe, Top2 requires repartitioning of strain along the helical axis to relax twist. Though relaxation is an energetically favored event, the extra energy from ATP-hydrolysis sharpens the distribution of relaxed products more than can be explained by a thermal Boltzmann partition function (Bates and Maxwell 2005;Podtelezhnikov et al 1999;Rybenkov et al 1997;Vologodskii 2009;Yan et al 1999). There are two major Top2s, Top2A and Top2B (Nitiss 2009).…”
mentioning
confidence: 99%