Conversion of DNA gyrase into a conventional type II topoisomerase

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Standard

Conversion of DNA gyrase into a conventional type II topoisomerase. / Kampranis, S C; Maxwell, A.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, No. 25, 10.12.1996, p. 14416-21.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kampranis, SC & Maxwell, A 1996, 'Conversion of DNA gyrase into a conventional type II topoisomerase', Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 25, pp. 14416-21.

APA

Kampranis, S. C., & Maxwell, A. (1996). Conversion of DNA gyrase into a conventional type II topoisomerase. Proceedings of the National Academy of Sciences of the United States of America, 93(25), 14416-21.

Vancouver

Kampranis SC, Maxwell A. Conversion of DNA gyrase into a conventional type II topoisomerase. Proceedings of the National Academy of Sciences of the United States of America. 1996 Dec 10;93(25):14416-21.

Author

Kampranis, S C ; Maxwell, A. / Conversion of DNA gyrase into a conventional type II topoisomerase. In: Proceedings of the National Academy of Sciences of the United States of America. 1996 ; Vol. 93, No. 25. pp. 14416-21.

Bibtex

@article{7a3b0a1cb2c6406395d44a6af90e7a97,
title = "Conversion of DNA gyrase into a conventional type II topoisomerase",
abstract = "DNA gyrase is unique among topoisomerases in its ability to introduce negative supercoils into closed-circular DNA. We have demonstrated that deletion of the C-terminal DNA-binding domain of the A subunit of gyrase gives rise to an enzyme that cannot supercoil DNA but relaxes DNA in an ATP-dependent manner. Novobiocin, a competitive inhibitor of ATP binding by gyrase, inhibits this reaction. The truncated enzyme, unlike gyrase, does not introduce a right-handed wrap when bound to DNA and stabilizes DNA crossovers; characteristics reminiscent of conventional type II topoisomerases. This new enzyme form can decatenate DNA circles with increased efficiency compared with intact gyrase and, as a result, can complement the temperature-sensitive phenotype of a parCts mutant. Thus these results suggest that the unique properties of DNA gyrase are attributable to the wrapping of DNA around the C-terminal DNA-binding domains of the A subunits and provide an insight into the mechanism of type II topoisomerases.",
keywords = "Animals, DNA, DNA Topoisomerases, Type II, Enzyme Activation, Nucleic Acid Conformation, Protein Conformation",
author = "Kampranis, {S C} and A Maxwell",
year = "1996",
month = dec,
day = "10",
language = "English",
volume = "93",
pages = "14416--21",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "25",

}

RIS

TY - JOUR

T1 - Conversion of DNA gyrase into a conventional type II topoisomerase

AU - Kampranis, S C

AU - Maxwell, A

PY - 1996/12/10

Y1 - 1996/12/10

N2 - DNA gyrase is unique among topoisomerases in its ability to introduce negative supercoils into closed-circular DNA. We have demonstrated that deletion of the C-terminal DNA-binding domain of the A subunit of gyrase gives rise to an enzyme that cannot supercoil DNA but relaxes DNA in an ATP-dependent manner. Novobiocin, a competitive inhibitor of ATP binding by gyrase, inhibits this reaction. The truncated enzyme, unlike gyrase, does not introduce a right-handed wrap when bound to DNA and stabilizes DNA crossovers; characteristics reminiscent of conventional type II topoisomerases. This new enzyme form can decatenate DNA circles with increased efficiency compared with intact gyrase and, as a result, can complement the temperature-sensitive phenotype of a parCts mutant. Thus these results suggest that the unique properties of DNA gyrase are attributable to the wrapping of DNA around the C-terminal DNA-binding domains of the A subunits and provide an insight into the mechanism of type II topoisomerases.

AB - DNA gyrase is unique among topoisomerases in its ability to introduce negative supercoils into closed-circular DNA. We have demonstrated that deletion of the C-terminal DNA-binding domain of the A subunit of gyrase gives rise to an enzyme that cannot supercoil DNA but relaxes DNA in an ATP-dependent manner. Novobiocin, a competitive inhibitor of ATP binding by gyrase, inhibits this reaction. The truncated enzyme, unlike gyrase, does not introduce a right-handed wrap when bound to DNA and stabilizes DNA crossovers; characteristics reminiscent of conventional type II topoisomerases. This new enzyme form can decatenate DNA circles with increased efficiency compared with intact gyrase and, as a result, can complement the temperature-sensitive phenotype of a parCts mutant. Thus these results suggest that the unique properties of DNA gyrase are attributable to the wrapping of DNA around the C-terminal DNA-binding domains of the A subunits and provide an insight into the mechanism of type II topoisomerases.

KW - Animals

KW - DNA

KW - DNA Topoisomerases, Type II

KW - Enzyme Activation

KW - Nucleic Acid Conformation

KW - Protein Conformation

M3 - Journal article

C2 - 8962066

VL - 93

SP - 14416

EP - 14421

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 25

ER -

ID: 159085660