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Further studies have confirmed our earlier observations that in the presence of EDTA, degradation of phage PBS2 [3H]uracil-labeled DNA is effected by an N-glycosidase activity in extracts of Bacillus subtilis that removes free uracil from DNA. In addition, such extracts contain a nuclease activity that attacks PBS2 DNA in the presence of CaCl2. The nuclease activity is not observed under conditions that inactivate N-glycosidase activity but does attack DNA that has been preincubated to remove uracil by N-glycosidase action. We therefore postulate that the nuclease requires N-glycosidase action to generate substrate for its activity, i.e., the nuclease appears to attack depyrimidinated sites rather than uracil sites in phage PBS2 DNA.
J Duncan, and
L Hamilton, and
E C Friedberg
April 1978,
Journal of bacteriology,
J Duncan, and
L Hamilton, and
E C Friedberg
June 1977,
Journal of virology,
J Duncan, and
L Hamilton, and
E C Friedberg
August 1977,
Journal of bacteriology,
J Duncan, and
L Hamilton, and
E C Friedberg
August 1975,
Journal of virology,
J Duncan, and
L Hamilton, and
E C Friedberg
April 1975,
Journal of bacteriology,
J Duncan, and
L Hamilton, and
E C Friedberg
May 1977,
The Journal of biological chemistry,
J Duncan, and
L Hamilton, and
E C Friedberg
September 1974,
Proceedings of the National Academy of Sciences of the United States of America,
J Duncan, and
L Hamilton, and
E C Friedberg
January 1979,
Cold Spring Harbor symposia on quantitative biology,
J Duncan, and
L Hamilton, and
E C Friedberg
October 1982,
Journal of bacteriology,
J Duncan, and
L Hamilton, and
E C Friedberg
January 1978,
Nucleic acids research,
