Kinetic and Thermodynamic Analysis of Mutant Type II DNA Topoisomerases That Cannot Covalently Cleave DNA
DNA topoisomerase II catalyzes two different chemical reactions as part of its DNA transport cycle: ATP hydrolysis and DNA breakage/religation. The coordination between these reactions was studied using mutants of yeast topoisomerase II that are unable to covalently cleave DNA. In the absence of DNA...
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Published in | The Journal of biological chemistry Vol. 274; no. 6; pp. 3446 - 3452 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
05.02.1999
American Society for Biochemistry and Molecular Biology |
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Abstract | DNA topoisomerase II catalyzes two different chemical reactions as part of its DNA transport cycle: ATP hydrolysis and DNA breakage/religation. The coordination between these reactions was studied using mutants of yeast topoisomerase II that are unable to covalently cleave DNA. In the absence of DNA, the ATPase activities of these mutant enzymes are identical to the wild type activity. DNA binding stimulates the ATPase activity of the mutant enzymes, but with steady-state parameters different from those of the wild type enzyme. These differences were examined through DNA binding experiments and pre-steady-state ATPase assays. One mutant protein, 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. Rapid chemical quench and pulse-chase ATPase experiments reveal that the mutant proteins bound to DNA have the same sequential hydrolysis reaction cycle as the wild type enzyme. Binding of ATP to the mutants is not notably impaired, but hydrolysis of the first ATP is slower than for the wild type enzyme. Models to explain these results in the context of the entire DNA topoisomerase II reaction cycle are discussed. |
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AbstractList | DNA topoisomerase II catalyzes two different chemical reactions as part of its DNA transport cycle: ATP hydrolysis and DNA
breakage/religation. The coordination between these reactions was studied using mutants of yeast topoisomerase II that are
unable to covalently cleave DNA. In the absence of DNA, the ATPase activities of these mutant enzymes are identical to the
wild type activity. DNA binding stimulates the ATPase activity of the mutant enzymes, but with steady-state parameters different
from those of the wild type enzyme. These differences were examined through DNA binding experiments and pre-steady-state ATPase
assays. One mutant protein, 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. Rapid chemical quench and pulse-chase ATPase experiments reveal that the mutant proteins bound to DNA have the
same sequential hydrolysis reaction cycle as the wild type enzyme. Binding of ATP to the mutants is not notably impaired,
but hydrolysis of the first ATP is slower than for the wild type enzyme. Models to explain these results in the context of
the entire DNA topoisomerase II reaction cycle are discussed. DNA topoisomerase II catalyzes two different chemical reactions as part of its DNA transport cycle: ATP hydrolysis and DNA breakage/religation. The coordination between these reactions was studied using mutants of yeast topoisomerase II that are unable to covalently cleave DNA. In the absence of DNA, the ATPase activities of these mutant enzymes are identical to the wild type activity. DNA binding stimulates the ATPase activity of the mutant enzymes, but with steady-state parameters different from those of the wild type enzyme. These differences were examined through DNA binding experiments and pre-steady-state ATPase assays. One mutant protein, 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. Rapid chemical quench and pulse-chase ATPase experiments reveal that the mutant proteins bound to DNA have the same sequential hydrolysis reaction cycle as the wild type enzyme. Binding of ATP to the mutants is not notably impaired, but hydrolysis of the first ATP is slower than for the wild type enzyme. Models to explain these results in the context of the entire DNA topoisomerase II reaction cycle are discussed. |
Author | Lindsley, Janet E. Morris, Shayne K. Harkins, Timothy T. Tennyson, Rachel B. |
Author_xml | – sequence: 1 givenname: Shayne K. surname: Morris fullname: Morris, Shayne K. – sequence: 2 givenname: Timothy T. surname: Harkins fullname: Harkins, Timothy T. – sequence: 3 givenname: Rachel B. surname: Tennyson fullname: Tennyson, Rachel B. – sequence: 4 givenname: Janet E. surname: Lindsley fullname: Lindsley, Janet E. email: Janet.Lindsley@hsc.utah.edu |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9920889$$D View this record in MEDLINE/PubMed |
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Snippet | DNA topoisomerase II catalyzes two different chemical reactions as part of its DNA transport cycle: ATP hydrolysis and DNA breakage/religation. The... DNA topoisomerase II catalyzes two different chemical reactions as part of its DNA transport cycle: ATP hydrolysis and DNA breakage/religation. The... |
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SubjectTerms | Adenosine Triphosphatases - metabolism Base Sequence DNA - metabolism DNA Primers DNA Topoisomerases, Type II - chemistry DNA Topoisomerases, Type II - metabolism Hydrolysis Kinetics Saccharomyces cerevisiae Thermodynamics |
Title | Kinetic and Thermodynamic Analysis of Mutant Type II DNA Topoisomerases That Cannot Covalently Cleave DNA |
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