PMID:9756859
| Citation |
Kampranis, SC and Maxwell, A (1998) Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase. J. Biol. Chem. 273:26305-9 |
|---|---|
| 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. |
| Links | |
| Keywords |
Adenosine Triphosphate/metabolism; Biopolymers; DNA Gyrase; DNA Topoisomerases, Type II/metabolism; DNA, Superhelical; Hydrolysis; Kinetics |
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