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. 1979 Dec;76(12):6289-93.
doi: 10.1073/pnas.76.12.6289.

DNA gyrase: purification and catalytic properties of a fragment of gyrase B protein

M Gellert, L M Fisher, M H O'Dea

DNA gyrase: purification and catalytic properties of a fragment of gyrase B protein

M Gellert et al. Proc Natl Acad Sci U S A. 1979 Dec.

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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References

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