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Partial purification and characterization of a uracil DNA N-glycosidase from Bacillus subtilis.

作者信息

Cone R, Duncan J, Hamilton L, Friedberg E C

出版信息

Biochemistry. 1977 Jul 12;16(14):3194-201. doi: 10.1021/bi00633a024.

DOI:10.1021/bi00633a024
PMID:407925
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) or uracil in DNA arising either by incorporation during DNA synthesis or by deamination of cytosine in DNA.

摘要

相似文献

1
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Uracil-DNA glycosylase defective mutants of Ustilago maydis.尿嘧啶-DNA 糖基化酶缺陷型突变体的构巢曲霉。
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DNA repair and genome maintenance in Bacillus subtilis.枯草芽孢杆菌中的 DNA 修复和基因组维护。
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Plant Physiol. 1987 Aug;84(4):1102-6. doi: 10.1104/pp.84.4.1102.
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