Catalysis of ATP hydrolysis by two NH(2)-terminal fragments of yeast DNA topoisomerase II (Q78037760)

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10 December 2019

title

Catalysis of ATP hydrolysis by two NH(2)-terminal fragments of yeast DNA topoisomerase II (English)

1 reference

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10 December 2019

author name string

S Olland

series ordinal

1

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10 December 2019

J C Wang

series ordinal

2

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10 December 2019

language of work or name

English

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publication date

1 July 1999

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Journal of Biological Chemistry

10 December 2019

published in

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10 December 2019

volume

274

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10 December 2019

issue

31

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10 December 2019

page(s)

21688-21694

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A topoisomerase from Escherichia coli related to DNA gyrase

10 December 2019

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DNA gyrase: subunit structure and ATPase activity of the purified enzyme

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T4 DNA topoisomerase: a new ATP-dependent enzyme essential for initiation of T4 bacteriophage DNA replication

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DNA transport by a type II DNA topoisomerase: evidence in favor of a two-gate mechanism

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Moving one DNA double helix through another by a type II DNA topoisomerase: the story of a simple molecular machine

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Crystal structure of an N-terminal fragment of the DNA gyrase B protein.

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The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs.

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Conformational changes in DNA gyrase revealed by limited proteolysis.

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DNA transport by a type II topoisomerase: direct evidence for a two-gate mechanism

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Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase

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The DNA Dependence of the ATPase Activity of Human DNA Topoisomerase IIα

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Energy coupling in DNA gyrase and the mechanism of action of novobiocin

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Nucleotide binding to the 43-kilodalton N-terminal fragment of the DNA gyrase B protein.

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The N-Terminal Domain of Human Topoisomerase IIα Is a DNA-Dependent ATPase†

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Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA.

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Proteolysis patterns of epitopically labeled yeast DNA topoisomerase II suggest an allosteric transition in the enzyme induced by ATP binding

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Footprinting of yeast DNA topoisomerase II lysyl side chains involved in substrate binding and interdomainal interactions

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Kinetic and thermodynamic analysis of mutant type II DNA topoisomerases that cannot covalently cleave DNA.

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