Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase

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Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase. / Kampranis, S C; Maxwell, A.

In: The Journal of Biological Chemistry, Vol. 273, No. 41, 09.10.1998, p. 26305-9.

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

Harvard

Kampranis, SC & Maxwell, A 1998, 'Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase', The Journal of Biological Chemistry, vol. 273, no. 41, pp. 26305-9.

APA

Kampranis, S. C., & Maxwell, A. (1998). Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase. The Journal of Biological Chemistry, 273(41), 26305-9.

Vancouver

Kampranis SC, Maxwell A. Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase. The Journal of Biological Chemistry. 1998 Oct 9;273(41):26305-9.

Author

Kampranis, S C ; Maxwell, A. / Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase. In: The Journal of Biological Chemistry. 1998 ; Vol. 273, No. 41. pp. 26305-9.

Bibtex

@article{374066d0232f4870bea5e67603921cce,
title = "Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase",
abstract = "Mutation of Glu42 to Ala in the B subunit of DNA gyrase abolishes ATP hydrolysis but not nucleotide binding. Gyrase complexes that contain one wild-type and one Ala42 mutant B protein were formed, and the ability of such complexes to hydrolyze ATP was investigated. We found that ATP hydrolysis was able to proceed independently only in the wild-type subunit, albeit at a lower rate. With only one ATP molecule hydrolyzed at a time, gyrase could still perform supercoiling, but the limit of this reaction was lower than that observed when both subunits can hydrolyze the nucleotide.",
keywords = "Adenosine Triphosphate, Biopolymers, DNA Gyrase, DNA Topoisomerases, Type II, DNA, Superhelical, Hydrolysis, Kinetics",
author = "Kampranis, {S C} and A Maxwell",
year = "1998",
month = oct,
day = "9",
language = "English",
volume = "273",
pages = "26305--9",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "41",

}

RIS

TY - JOUR

T1 - Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase

AU - Kampranis, S C

AU - Maxwell, A

PY - 1998/10/9

Y1 - 1998/10/9

N2 - Mutation of Glu42 to Ala in the B subunit of DNA gyrase abolishes ATP hydrolysis but not nucleotide binding. Gyrase complexes that contain one wild-type and one Ala42 mutant B protein were formed, and the ability of such complexes to hydrolyze ATP was investigated. We found that ATP hydrolysis was able to proceed independently only in the wild-type subunit, albeit at a lower rate. With only one ATP molecule hydrolyzed at a time, gyrase could still perform supercoiling, but the limit of this reaction was lower than that observed when both subunits can hydrolyze the nucleotide.

AB - Mutation of Glu42 to Ala in the B subunit of DNA gyrase abolishes ATP hydrolysis but not nucleotide binding. Gyrase complexes that contain one wild-type and one Ala42 mutant B protein were formed, and the ability of such complexes to hydrolyze ATP was investigated. We found that ATP hydrolysis was able to proceed independently only in the wild-type subunit, albeit at a lower rate. With only one ATP molecule hydrolyzed at a time, gyrase could still perform supercoiling, but the limit of this reaction was lower than that observed when both subunits can hydrolyze the nucleotide.

KW - Adenosine Triphosphate

KW - Biopolymers

KW - DNA Gyrase

KW - DNA Topoisomerases, Type II

KW - DNA, Superhelical

KW - Hydrolysis

KW - Kinetics

M3 - Journal article

C2 - 9756859

VL - 273

SP - 26305

EP - 26309

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 41

ER -

ID: 159085598