ATP-dependent DNA topoisomerase from D. melanogaster reversibly catenates duplex DNA rings
TLDR
It is shown that the ATP-dependent DNA topoisomerase relaxes DNA by a mechanism distinct from that of nicking-closing enzymes, which could be useful in relaxation of topological constraints, but also may be involved in the folding and unfolding of eucaryotic chromosomes.About:
This article is published in Cell.The article was published on 1980-08-01 and is currently open access. It has received 262 citations till now. The article focuses on the topics: DNA supercoil & DNA clamp.read more
Citations
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Journal ArticleDOI
DNA Topoisomerases: Essential Enzymes and Lethal Targets
Allan Y. Chen,Leroy F. Liu +1 more
TL;DR: The discovery of E. coli topoisomerase I led to the proposal that the enzyme may form a high-energy covalent bond between itself and the transiently broken DNA phosphodiester bond, and these predictions have turned out to be correct.
Journal ArticleDOI
DNA topoisomerase II is required at the time of mitosis in yeast
TL;DR: Five new temperature-sensitive DNA topoisomerase II mutations are constructed and their physiological consequences in yeast are analyzed, consistent with the hypothesis that the essential function of topoisomersase II is to allow the separation of intertwined chromosomal DNA molecules during mitosis.
Journal ArticleDOI
DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe.
Tadashi Uemura,Hiroyuki Ohkura,Yasuhisa Adachi,Kazuhiko Morino,Kazuhiro Shiozaki,Mitsuhiro Yanagida +5 more
TL;DR: It is shown that DNA topoisomerase II (topo II) is continuously required for mitotic chromosome changes in Schizosaccharomyces pombe and pulse-shift experiments show that topo II is required for chromatid disjuction.
Journal ArticleDOI
The SV40 72 base repair repeat has a striking effect on gene expression both in SV40 and other chimeric recombinants
TL;DR: The possibility that the 72 bp repeat region in SV40 may act as a bi-directional entry site for RNA polymerase B such that promoter sequences linked to the repeat are more efficiently utilised is discussed.
Journal Article
Inhibitory Effects of the Tyrosine Kinase Inhibitor Genistein on Mammalian DNA Topoisomerase II
Judith Markovits,Linassier C,Philippe Fossé,Couprie J,Josiane Pierre,A. Jacquemin-Sablon,Jean-Marie Saucier,Le Pecq Jb,Annette K. Larsen +8 more
TL;DR: The results show that genistein is an inhibitor of both protein tyrosine kinases and mammalian DNA topoisomerase II, accounted for by the sharing of a common structure sequence between the two proteins at the ATP binding site.
References
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Book ChapterDOI
[31] Electron microscope heteroduplex methods for mapping regions of base sequence homology in nucleic acids
Journal ArticleDOI
DNA gyrase: an enzyme that introduces superhelical turns into DNA
TL;DR: Relaxed closed-circular DNA is converted to negatively supercoiled DNA by DNA gyrase by purified from Escherichia coli cells, and the final superhelix density of the DNA can be considerably greater than that found in intracellularly super coiled DNA.
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Nalidixic acid resistance: A second genetic character involved in DNA gyrase activity
TL;DR: The nalA locus is responsible for a second component needed for DNA gyrase activity in addition to the component determined by the previously described locus for resistance to novobiocin and coumermycin (cou), which appears to be involved in the nicking-closing activity required in the supercoiling reaction.
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Mechanism of action of nalidixic acid: Purification of Escherichia coli nalA gene product and its relationship to DNA gyrase and a novel nicking-closing enzyme
TL;DR: It is postulate that the nalA gene product occurs in two molecular forms, as Pnal and as a gyrase component, and inhibition of this activity by nalidixic and oxolinic acids may account for the inhibition of DNA synthesis by these drugs.
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Interaction between DNA and an Escherichia coli protein ω
TL;DR: It appears that ω is capable of introducing a “swivel” reversibly into a DNA, and a plausible mechanism is postulated.