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Information on EC 5.6.2.2 - DNA topoisomerase (ATP-hydrolysing) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P06786
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5.6.2.2 DNA topoisomerase (ATP-hydrolysing)IUBMB Comments
The enzyme can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyses super-twisting and hydrolysis of ATP (cf. EC 5.6.2.1 DNA topoisomerase).
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Word Map
- 5.6.2.2
- myosin
- na+
- adp
- sarcoplasmic
- cardiac
- actin
- etoposide
- helicase
- chromatin
- strand
- triphosphatase
- ouabain
-
multidrug
-
supercoiling
- leukemia
-
contractile
- fiber
- doxorubicin
- erythrocyte
- p-glycoprotein
-
single-stranded
-
poison
-
quinolone
- myofibrillar
- vanadate
- fluoroquinolones
- actomyosin
- ciprofloxacin
-
unwind
- microtubule
- duplex
- hsp90
- vacuolar
-
dna-dependent
- calmodulin
- serca
- anthracyclines
-
ca2+-dependent
- camptothecin
- myofibril
- thapsigargin
- kinesins
- verapamil
- nucleosome
- troponin
- dyneins
- fork
-
sliding
-
isometric
-
electrogenic
- medicine
- diagnostics
- analysis
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
atpase, topoisomerase ii, dna gyrase, topo ii, gyrase, top2a, dna topoisomerase ii, topoisomerase iialpha, topo iialpha, topoisomerase ii alpha, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DNA gyrase
-
-
-
-
DNA topoisomerase II
DNA topoisomerase type II
-
-
-
-
Isomerase, deoxyribonucleate topo-, II
-
-
-
-
NP170 proteins
-
-
-
-
Nuclear proteins 170,000-mol.wt.
-
-
-
-
Protein Gp39
-
-
-
-
Protein Gp52
-
-
-
-
Protein Gp60
-
-
-
-
Proteins , NP170 (specific proteins and subclasses nuclear protein, 170,000-mol.-wt.)
-
-
-
-
PsTopII
-
-
-
-
TOPOII
Topoisomerase II
Topoisomerase type II
-
-
-
-
Type II-DNA-topoisomerase
-
-
-
-
DNA topoisomerase II
-
-
-
-
TOPOII
-
-
-
-
Topoisomerase II
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP-dependent breakage, passage and rejoining of double-stranded DNA
model in which the DNA-bound enzyme acts as an ATP-operated clamp for the capture and transport of a second DNA segment
-
ATP-dependent breakage, passage and rejoining of double-stranded DNA
reaction mechanism, overview
-
ATP-dependent breakage, passage and rejoining of double-stranded DNA
metal-dependent general acid-base catalysis, quantum mechanical/molecular mechanical calculations for the topo II religation reaction, substrate-mediated proton transfer pathway, which involves the 3'-OH nucleophile, the reactive phosphate, water, Arg781, and Tyr782, metal A stabilizes the transition states, which is consistent with a two-metal mechanism in topo II, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
DNA topoisomerase (ATP-hydrolysing)
The enzyme can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyses super-twisting and hydrolysis of ATP (cf. EC 5.6.2.1 DNA topoisomerase).
CAS REGISTRY NUMBER
COMMENTARY
142805-56-9
-
80449-01-0
formerly not distinguished from EC 5.99.1.2
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + ATP
?
-
decatenation, the enzyme normally catalyzes DNA transport after it hydrolyzes one ATP and before it hydrolyzes the second
-
?
DNA + ATP + H2O
DNA + ADP + phosphate
-
relaxation and cleavage of DNA, cleavage requires coupling to ATP hydrolysis
-
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
in absence of an DNA-binding protein: decatenation and unknotting of the DNA rings
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
network of DNA rings that are topologically interlocked
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
in presence of a yeast DNA-binding protein
network of DNA rings that are topologically interlocked
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
covalently closed double-stranded DNA rings
network of DNA rings that are topologically interlocked
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively supercoiled DNA
-
?
additional information
?
-
DNA cleavage, aperture, closure and religation are critical steps in the topo II reaction cycle, topo II DNA gate dynamics, single-molecule FRET experiments, role of T-segment in gate opening, overview
-
-
?
additional information
?
-
-
changes the linking number of a closed circular molecule by integers
-
-
?
additional information
?
-
-
characterization of the interaction of topoisomerase II with DNA and identification of a DNA-binding domain, conserved DNA-binding mechanism
-
-
?
additional information
?
-
-
the enzyme performs ATP hydrolysis activity
-
-
?
additional information
?
-
-
topoisomerase II relaxes nucleosomal DNA much faster than topoisomerase I, and the DNA cross-inversion mechanism of topomerase II is facilitated in chromatin. Enzyme is the main modulator of DNA topology in chromatin fibers
-
-
?
additional information
?
-
-
G-DNA binds with higher affinity than T-DNA. enzyme with only G-DNA bound is competent to cleave DNA and the ATPase activity of enzyme solely bound to G-DNA is partially stimulated. Full stimulation requires binding of T-DNA
-
-
?
additional information
?
-
-
the sequence that defines a cleavage site resides within the central 20 bp of a dNA duplex. The DNA affinity does not correlate with the ability of the enzyme to cleave DNA. The binding step does not contribute significantly to the selection mechanism
-
-
?
additional information
?
-
-
Top2 plays a role in centromeric chromatin compaction
-
-
?
additional information
?
-
-
the enzyme introduces transient double strand breaks to alter DNA topology, generation of a transient double strand break, with each subunit breaking one DNA strand. The mechanism of DNA cleavage provides several distinct advantages including the protection of DNA ends and the ability to quickly and efficiently religate the DNA strand break. The positively supercoiled DNA at the replication fork can isomerize by migration of the positive supercoiling into wrapping of the two replicated strands. This structure called a precatenane, is a substrate for Top2 mediated DNA catenation, and may represent a plausible mechanism for Top2 action during replication elongation
-
-
?
additional information
?
-
-
reaction mechanism, DNA cleavage by Top2 uses a tyrosine that is activated to attack the phosphodiester backbone of DNA and form a phosphotyrosine linkage, overview
-
-
?
additional information
?
-
-
substrate is negatively-supercoiled plasmid DNA
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
topoisomerase II relaxes nucleosomal DNA much faster than topoisomerase I, and the DNA cross-inversion mechanism of topomerase II is facilitated in chromatin. Enzyme is the main modulator of DNA topology in chromatin fibers
-
-
?
additional information
?
-
-
Top2 plays a role in centromeric chromatin compaction
-
-
?
additional information
?
-
-
the enzyme introduces transient double strand breaks to alter DNA topology, generation of a transient double strand break, with each subunit breaking one DNA strand. The mechanism of DNA cleavage provides several distinct advantages including the protection of DNA ends and the ability to quickly and efficiently religate the DNA strand break. The positively supercoiled DNA at the replication fork can isomerize by migration of the positive supercoiling into wrapping of the two replicated strands. This structure called a precatenane, is a substrate for Top2 mediated DNA catenation, and may represent a plausible mechanism for Top2 action during replication elongation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis
ATP
-
all nonsupercoiling type II topoisomerases require ATP hydrolysis for relaxation
ATP
-
the N-terminal domain of the protein carries the ATP binding domain consisting of a GHKL fold
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
absolute requirement for a divalent cation, Mg2+ is the most effective. Mn2+, Ca2+, or Co2+ support the reaction to a lesser extent
Co2+
-
absolute requirement for a divalent cation, Mg2+ is the most effective. Mn2+, Ca2+, or Co2+ support the reaction to a lesser extent
K+
-
decatenation reaction proceedes efficiently only at concentrations above 150 mM KCl
Mg2+
Mn2+
-
absolute requirement for a divalent cation, Mg2+ is the most effective. Mn2+, Ca2+, or Co2+ support the reaction to a lesser extent
Mg2+
-
absolute requirement for a divalent cation, Mg2+ is the most effective. Mn2+, Ca2+, or Co2+ support the reaction to a lesser extent
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,3R)-8-methoxy-1-methyl-5,10-dioxo-3,4,5,10-tetrahydro-1H-benzo[g]isochromene-3-carboxylic acid
-
-
(1R,3S)-1,3,8-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(1R,3S)-7,9-dimethoxy-1,3,6-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-3-methyl-7,9-bis(propan-2-yloxy)-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-7,9-dihydroxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-7,9-dimethoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-9-hydroxy-7-methoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
ADP
-
traps the wild-type enzyme in the closed clamp formation, which shows no ATPAse hydrolysis activity
AMP-PNP
-
structure analysis of a fully-catalytic Saccharomyces cerevisiae topoisomerase II homodimer complexed with DNA and the nonhydrolyzable ATP analogue, overview. The enzyme adopts a domain-swapped configuration wherein the ATPase domain of one protomer sits atop the nucleolytic region of its partner subunit. This organization produces an unexpected interaction between the bound DNA and a conformational transducing element in the ATPase domain, which is critical for both DNA-stimulated ATP hydrolysis and global topoisomerase activity. Three dimerization interfaces can each exist in an associated or dissociated state, giving rise to significant conformational variability within a population
bisdioxopiperazine
-
inhibits the ATPase activity of the wild-type enzyme
ellipticines
-
mechanism of drug action, characterization of the interaction between ellipticine and the enzyme
etoposide
-
geminal protons of the A-ring, the H5 and H8 protons of the B-ring, and the H2 and H6 protons and the 3- and 5-methoxyl protons of the pendent E-ring interact with enzyme in the binary protein-ligand complex. No significant nuclear Overhauser enhancement signals arise from the C-ing, the D-ring, or the C4 glycosidic moiety
Peptide fragments of DNA topoisomerase II with helix-forming and coiled-coil-forming properties
-
-
-
sodium orthovanadate
-
noncompetitive, formation of a ternary enzyme-ADP-vanadate complex, inhibits the ATPase activity of the wild-type enzyme, traps the enzyme in a salt-stable closed conformation, i.e. the closed clamp, no inhibition of mutant Y28F
additional information
-
no inhibition by nalidixic acid, oxolinic acid or novobiocin
-
additional information
-
cytotoxicity of eleutherin and pyranonaphthoquinone derivatives, structure-activity study and mechanism, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DNA
-
stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
ATP hydrolysis kinetics for wild-type and Y28F mutant enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
ATP
-
pH 7.7, 30°C, recombinant Y50F mutant enzyme, in absence of DNA
1.1
ATP
-
pH 7.7, 30°C, recombinant wild-type enzyme, in absence of DNA
1.2
ATP
-
pH 7.7, 30°C, recombinant Y50F mutant enzyme, in presence of DNA
3.6
ATP
-
pH 7.7, 30°C, recombinant wild-type enzyme, in presence of DNA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
topoisomerase II poisons generate DNA damage, in addition to inhibition of enzyme activity, and cause delay of cell cycle progression due to DNA damage checkpoints
physiological function
additional information
-
the K-loop couples DNA binding to ATPase activity
physiological function
-
Top2 functions, such as DNA replication, transcription and chromosome segregation, are processes that are essential for preventing tumorigenesis. Top2 plays a key role in chromosome structure and chromosome condensation
physiological function
-
centromeric plasmids undergo a dramatic change in their topology as the cells pass through mitosis. This change is characterized by positive supercoiling of the DNA and requires mitotic spindles and the condensin factor Smc2. When mitotic positive supercoiling occurs on decatenated DNA, it is rapidly relaxed by topoisomerase II. DNA topoisomerase II completely removes DNA intertwining, or catenation, between sister chromatids before they are segregated during cell division. However, when positive supercoiling takes place in catenated plasmid, topoisomerase II activity is directed toward decatenation of the molecules before relaxation. The topological change on DNA drives topoisomerase II to decatenate molecules during mitosis, potentially driving the full decatenation of the genome, mechanism, overview. Once the sister chromatids are fully decatenated, topoisomerase II rapidly relaxes the positive supercoiling generated, returning the intrachromosomal topology of the sister chromatids to a state comparable to that observed before the transition, except that now, crucially, all catenated links have been removed
physiological function
-
type IIA topoisomerases control DNA supercoiling and disentangle chromosomes by a complex, ATP-dependent strand passage mechanism, control mechanism for ATPase activity, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
150000
-
1 * or 2 * 150000, the proportions of monomers and dimers in the monomer-dimer equilibrium strongly depends on both the protein concentration and the salt concentration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
homodimer
monomer
-
1 * or 2 * 150000, the proportions of monomers and dimers in the monomer-dimer equilibrium strongly depends on both the protein concentration and the salt concentration
additional information
-
stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis
dimer
determination and analysis of N- nad C-terminal fragments, comparison to the human enzyme, overview. The N-terminal region bears the characteristic GHKL ATP-binding fold, while the C-terminal region comprises the transducer domain
dimer
determination and analysis of N- and C-terminal fragments, comparison to the human enzyme, overview. The N-terminal region bears the characteristic GHKL ATP-binding fold, while the C-terminal region comprises the transducer domain
dimer
-
1 * or 2 * 150000, the proportions of monomers and dimers in the monomer-dimer equilibrium strongly depends on both the protein concentration and the salt concentration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular model of the entire enzyme in complex with DNA after the cleavage reaction. Anthracycline antibiotics contact specifically the cleaved DNA as well as amino acid residues of the enzyme CAP-like domain
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y28F
-
site-directed mutagenesis, mutation of an ATP hydrolysis domain residue of a bisdioxopiperazine- and sodium orthovanadate-resistant mutant enzyme, mutant shows reduced DNA-dependent ATP-hydrolysis activity without affecting the relaxation activity of the enzyme, no formation of the closed clamp conformation with vanadate or ADP, but with ADP-PNP
Y782F
additional information
Y782F
-
binds DNA with the same affinity as wild-type protein. This mutant topologically traps one DNA circle in the presence of a nonhydrolyzable ATP analog under the same conditions that the wild type protein catenates two circles. The mutant enzyme has the same sequential hydrolysis reaction cycle as the wild-type enzyme, hydrolysis of the first ATP is slower than for the wild-type enzyme
Y782F
-
mutation within the G-DNA binding site. Mutation affects DNA cleavage but has negligible effects on steady state ATP hydrolysis
additional information
-
two mutants resistant to etoposide and amsacrine, and a third mutant partially resistant to etoposide and fluoroquinoline but not the amsacrine, that has an amino acid change at position 738
additional information
-
catalytically inactive Top2 generates DNA damage before mitosis
additional information
-
Top2 promotes tension checkpoint arrest and chromatid detachment in Mtw1 mutants with affected kinetochore protein Mtw1
additional information
-
cells depleted of Top2 can complete replication, but not chromosome decatenation, and lose viability at mitosis, Top2 depeletion phenotype, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of full-length Saccharomyces cerevisiae topoisomerase II fused to an intein and a chitin binding domain affinity tag in the yeast strain BCY123
-
overexpression of wild-type and mutant enzyme in yeast JELt1 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goto, T.; Laipis, P.; Wang, J.C.
The purification and characterization of DNA topoisomerases I and II of the yeast Saccharomyces cerevisiae
J. Biol. Chem.
259
10422-10429
1984
Saccharomyces cerevisiae
Andersen, A.H.; Bendixen, C.; Westergaard, O.
DNA topoisomerases
DNA Replication in eucaryotic cells, Cold Spring Harbor Laboratory Press
587-617
1996
Bacteria, Saccharomyces cerevisiae, eukaryota, Homo sapiens, Mus musculus
-
Goto, T.; Wang, J.C.
Yeast DNA topoisomerase II
J. Biol. Chem.
257
5866-5872
1982
Saccharomyces cerevisiae
Insaf, S.; Danks, M.K.; Witiak, D.T.
Structure-function analysis of DNA topoisomerase II inhibitors
Curr. Med. Chem.
3
437-466
1996
Saccharomyces cerevisiae, eukaryota, Homo sapiens, Mammalia
-
Lamhasni, S.; Larsen, A.K.; Barray, M.; Monnot, M.; DeLain, E.; Fermandjian, S.
Changes of self-association, secondary structure, and biological activity properties of topoisomerase II under varying salt conditions
Biochemistry
34
3632-3639
1995
Saccharomyces cerevisiae
Hung, F.; Luo, D.; Sauve, D.M.; Muller, M.T.; Roberge, M.
Characterization of topoisomerase II-DNA interaction and identification of a DNA-binding domain by ultraviolet laser crosslinking
FEBS Lett.
380
127-132
1996
Saccharomyces cerevisiae
Frere-Gallois, V.; Krebs, D.; Scala, D.; Troalen, F.; Fermandjian, S.
Peptide fragments of DNA topoisomerase II with helix-forming and coiled-coil-forming properties act as inhibitors of the enzyme
Eur. J. Biochem.
249
142-148
1979
Saccharomyces cerevisiae
Froehlich-Ammon, S.J.; Patchan, M.W.; Osheroff, N.; Thompson, R.B.
Topoisomerase II binds to ellipticine in the absence or presence of DNA. Characterization of enzyme-drug interactions by fluorescence spectroscopy
J. Biol. Chem.
270
14998-15004
1995
Saccharomyces cerevisiae
Liu, Y.X.; Hsiung, Y.; Jannatipour, M.; Yeh, Y.; Nitiss, J.L.
Yeast topoisomerase II mutants resistant to anti-topoisomerase agents: identification and characterization of new yeast topoisomerase II mutants selected for resistance to etoposide
Cancer Res.
54
2943-2951
1994
Saccharomyces cerevisiae
Lindsley, J.E.; Wang, J.C.
On the coupling between ATP usage and DNA transport by yeast DNA topoisomerase II
J. Biol. Chem.
268
8096-8104
1993
Saccharomyces cerevisiae
Morris, S.K.; Harkins, T.T.; Tennyson, R.B.; Lindsley, J.E.
Kinetic and thermodynamic analysis of mutant type II DNA topoisomerases that cannot covalently cleave DNA
J. Biol. Chem.
274
3446-3452
1999
Saccharomyces cerevisiae
Baird, C.L.; Harkins, T.T.; Morris, S.K.; Lindsley, J.E.
Topoisomerase II drives DNA transport by hydrolyzing one ATP
Proc. Natl. Acad. Sci. USA
96
13685-13690
1999
Saccharomyces cerevisiae
Vaughn, J.; Huang, S.; Wessel, I.; Sorensen, T.K.; Hsieh, T.; Jensen, L.H.; Jensen, P.B.; Sehested, M.; Nitiss, J.L.
Stability of the topoisomerase II closed clamp conformation may influence DNA-stimulated ATP hydrolysis
J. Biol. Chem.
280
11920-11929
2005
Saccharomyces cerevisiae, Homo sapiens
Wilstermann, A.M.; Bender, R.P.; Godfrey, M.; Choi, S.; Anklin, C.; Berkowitz, D.B.; Osheroff, N.; Graves, D.E.
Topoisomerase II - drug interaction domains: identification of substituents on etoposide that interact with the enzyme
Biochemistry
46
8217-8225
2007
Saccharomyces cerevisiae, Homo sapiens
Dal Ben, D.; Palumbo, M.; Zagotto, G.; Capranico, G.; Moro, S.
DNA topoisomerase II structures and anthracycline activity: insights into ternary complex formation
Curr. Pharm. Des.
13
2766-2780
2007
Saccharomyces cerevisiae
Salceda, J.; Fernandez, X.; Roca, J.
Topoisomerase II, not topoisomerase I, is the proficient relaxase of nucleosomal DNA
EMBO J.
25
2575-2583
2006
Saccharomyces cerevisiae
Mueller-Planitz, F.; Herschlag, D.
Interdomain communication in DNA topoisomerase II. DNA binding and enzyme activation
J. Biol. Chem.
281
23395-23404
2006
Saccharomyces cerevisiae
Mueller-Planitz, F.; Herschlag, D.
DNA topoisomerase II selects DNA cleavage sites based on reactivity rather than binding affinity
Nucleic Acids Res.
35
3764-3773
2007
Saccharomyces cerevisiae
Stuchinskaya, T.; Mitchenall, L.A.; Schoeffler, A.J.; Corbett, K.D.; Berger, J.M.; Bates, A.D.; Maxwell, A.
How do type II topoisomerases use ATP hydrolysis to simplify DNA topology beyond equilibrium? Investigating the relaxation reaction of nonsupercoiling type II topoisomerases
J. Mol. Biol.
385
1397-1408
2008
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Warsi, T.H.; Navarro, M.S.; Bachant, J.
DNA topoisomerase II is a determinant of the tensile properties of yeast centromeric chromatin and the tension checkpoint
Mol. Biol. Cell
19
4421-4433
2008
Saccharomyces cerevisiae
Baxter, J.; Diffley, J.F.
Topoisomerase II inactivation prevents the completion of DNA replication in budding yeast
Mol. Cell
30
790-802
2008
Saccharomyces cerevisiae
Sperry, J.; Lorenzo-Castrillejo, I.; Brimble, M.A.; Machin, F.
Pyranonaphthoquinone derivatives of eleutherin, ventiloquinone L, thysanone and nanaomycin A possessing a diverse topoisomerase II inhibition and cytotoxicity spectrum
Bioorg. Med. Chem.
17
7131-7137
2009
Saccharomyces cerevisiae, Homo sapiens
Nitiss, J.L.
DNA topoisomerase II and its growing repertoire of biological functions
Nat. Rev. Cancer
9
327-337
2009
Saccharomyces cerevisiae, Homo sapiens
Collins, T.R.; Hammes, G.G.; Hsieh, T.S.
Analysis of the eukaryotic topoisomerase II DNA gate: a single-molecule FRET and structural perspective
Nucleic Acids Res.
37
712-720
2009
Homo sapiens, Saccharomyces cerevisiae (P06786)
Baxter, J.; Sen, N.; Lopez Martinez, V.; Monturus De Carandini, M.; Schvartzman, J.; Diffley, J.; Aragon, L.
Positive supercoiling of mitotic DNA drives decatenation by topoisomerase II in eukaryotes
Science
331
1328-1332
2011
Saccharomyces cerevisiae
Hanaoka, K.; Shoji, M.; Kondo, D.; Sato, A.; Yang, M.Y.; Kamiya, K.; Shiraishi, K.
Substrate-mediated proton relay mechanism for the religation reaction in topoisomerase II
J. Biomol. Struct. Dyn.
32
1759-1765
2013
Saccharomyces cerevisiae
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