Partial Purification and Characterization of a Uracil DNA N-Glycosidase from Bacillus subtilis

Richard Cone, James Duncan, Lenore Hamilton, Errol C. Friedberg

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

Abstract

A uracil specific DNA N-glycosidase activity has been partially purified from crude extracts of Bacillus subtilis. The enzyme has a molecular weight of approximately 24 000 with no subunit structure. It has no requirement for any known cofactors but is inhibited in the presence of Co2+, Fe2+, or Zn2+. The enzyme is specific for uracil in single- and double-stranded deoxyribonucleopolymers and does not release free uracil from RNA or from poly(rU):poly(dA). In addition, neither Udr, dUMP, nor dUTP is recognized as substrate. The enzyme will attack small poly(dU) oligomers but the minimum size recognized as substrate is (pU)4. This enzyme may have a role in the repair (by base excision) of uracil in DNA arising either by incorporation during DNA synthesis or by deamination of cytosine in DNA.

Original languageEnglish (US)
Pages (from-to)3194-3201
Number of pages8
JournalBiochemistry
Volume16
Issue number14
DOIs
StatePublished - Jul 1 1977

ASJC Scopus subject areas

  • Biochemistry

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