PMID:230505
| Citation |
Gellert, M, Fisher, LM and O'Dea, MH (1979) DNA gyrase: purification and catalytic properties of a fragment of gyrase B protein. Proc. Natl. Acad. Sci. U.S.A. 76:6289-93 |
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| Abstract |
A protein isolated from Escherichia coli complements the DNA gyrase A (NalA) protein to generate an activity that relaxes supercoiled DNA. Oxolinic acid, a known inhibitor of DNA gyrase, blocks this activity and causes double-strand cleavage of DNA at the same sites as are attacked by DNA gyrase. The protein, of molecular weight 50,000, appears to be fragment of the DNA gyrase B (Cou) protein (molecular weight, 90,000) as judged by the identical sizes of numerous peptides produced by partial proteolytic digestion. The complex of this fragment and the gyrase A protein lacks both the DNA-supercoiling and DNA-dependent ATPase activities of DNA gyrase. |
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| Keywords |
Catalysis; DNA Topoisomerases, Type II/isolation & purification; DNA Topoisomerases, Type II/metabolism; DNA, Superhelical/pharmacology; Endonucleases/metabolism; Escherichia coli/enzymology; Macromolecular Substances; Molecular Weight; Oxolinic Acid/pharmacology; Topoisomerase II Inhibitors |
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