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

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

SN - 0021-9258

VL - 273

SP - 26305

EP - 26309

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

IS - 41

ER -