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

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

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26 Citations (Scopus)

Abstract

Further studies have confirmed earlier observation that in the presence of EDTA, degradation of phage BPS2 [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. The authors 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.

Original languageEnglish (US)
Pages (from-to)338-345
Number of pages8
JournalJournal of Virology
Volume19
Issue number2
StatePublished - 1976

Fingerprint

uracil
Uracil
nucleases
glycosidases
Glycoside Hydrolases
Bacillus subtilis
degradation
DNA
extracts
bacteriophages
Bacteriophages
Uracil-DNA Glycosidase
Edetic Acid
Observation

ASJC Scopus subject areas

  • Immunology

Cite this

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abstract = "Further studies have confirmed earlier observation that in the presence of EDTA, degradation of phage BPS2 [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. The authors 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.",
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AB - Further studies have confirmed earlier observation that in the presence of EDTA, degradation of phage BPS2 [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. The authors 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.

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