Author:
Duncan J,Hamilton L,Friedberg E C
Abstract
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.
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Reference13 articles.
1. Deoxynucleotide-polymerizing enzymes of calf thymut gland. V. Homogeneous terminal deoxynucleotidyl transferase;Chang L. M. S.;J. Biol. Chem.,1971
2. N-glycosidase activity in extracts ofBacillus subtilis and its inhibition after infection with bacteriophage PBS2;Friedberg E. C.;J. Virol.,1975
3. Endonuclease II ofE. coli. I. Isolation and purification;Friedberg E. C.;Proc. Natl. Acad. Sci. U.S.A.,1969
4. Molecular weight of bacteriophage PBS2 deoxyribonucleic acid;Hunter B. I.;J. Virol.,1967
5. Kirtikar D. M. J. P. Kuebler A. Dipple. and D. A. Goldthwait. 1976. Enzymes involved in repair of DNA damaged by chemical carcinogens and y-irradiation. In J. Schultz and F. Ahmad (ed.) Cancer enzymology - 8th Miami winter symposium. In press. Academic Press New York.
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