ATP-dependent deoxyribonuclease in Bacillus subtilis and a mutant deficient in this activity |
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Authors: | J Doly E Sasarman C Anagnostopoulos |
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Institution: | Centre de Génétique Moléculaire, C.N.R.S., 91190-Gif-sur-Yvette France |
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Abstract: | ATP-dependent DNAse activity was measured in rec+ and several rec strains of B. subtilis 168. One of the strains (marker recE5) was found to lack this activity. The enzyme from the wild type was partially purified and some of its properties were determined. The pH optimum is 9.5. Activity is higher at 50° but inactivation occurs on standing at this temperature. The enzyme requires Mg2+ (10?2M) or Mn2+ (2·10?4M). ATP is an absolute requirement and the only other nucleoside triphosphate that can partially replace it is dATP. Lack of activity in the mutant does not seem to be due to the presence of an inhibitor. Results so far do not allow us to conclude as to whether or not the mutant produces an altered enzyme. |
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Keywords: | DTT dithiothreitol TCA trichloroacetic acid |
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