Adenosine Triphosphatase Associated with Adenosine Triphosphate-Dependent Deoxyribonuclease

F. G. Nobrega*,
F. H. Rola†,
M. Pasetto-Nobrega*, and
M. Oishi

¹The Public Health Research Institute of the City of New York, Inc., New York, N.Y. 10016

Abstract

An ATPase activity that is completely dependent on DNA is associated with the ATP-dependent DNase (recB-recC enzyme) purified from Escherichia coli. There is a strong correlation between the ATPase and the DNase activities under various assay conditions. With E. coli DNA as substrate, 8-9 molecules of ATP are hydrolyzed to ADP and inorganic phosphate for every phosphodiester bond hydrolyzed by the DNase. The possible functional relationship of the ATPase and DNase activities is discussed.

recB-recC enzyme
E. coli
ATP to phosphodiester hydrolysis ratio
DNA-dependent ATPase activity

Footnotes

↵ * Present address: Departmento de Bioquimica, Instituto de Quimica, Caixa Postal 20780, Säo Paulo, Brazil.
↵ † Present address: Instituto de Biologia, Fortaleza, Ceara, Brazil.