Enzymatic degradation of uracil-containing DNA. II. Evidence of N-glycosidase and nuclease activities in unfractionated extracts of Bacillus subtilis

Journal Article · Sun Aug 01 04:00:00 EDT 1976 · J. Virol.; (United States)

OSTI ID:7156172

Duncan, J; Hamilton, L; Friedberg, E C

Further studies have confirmed our earlier observation that in the presence of EDTA, degradation of phage PBS2 (/sup 3/H)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 CaCl/sub 2/. 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.

• Research Organization: Stanford Univ., CA
• OSTI ID: 7156172
• Journal Information: J. Virol.; (United States), Journal Name: J. Virol.; (United States) Vol. 19:2; ISSN JOVIA
• Country of Publication: United States
• Language: English

Related Subjects

550500* -- Metabolism
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
AZINES
BACILLUS
BACILLUS SUBTILIS
BACTERIA
BACTERIOPHAGES
BIOLOGICAL EFFECTS
CARBOXYLIC ACIDS
CHELATING AGENTS
CHEMICAL REACTIONS
DECOMPOSITION
DNA
EDTA
ENZYMES
HETEROCYCLIC COMPOUNDS
HYDROXY COMPOUNDS
METABOLISM
MICROORGANISMS
NUCLEASES
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PARASITES
PHOSPHOTRANSFERASES
PYRIMIDINES
TRANSFERASES
URACILS
VIRUSES