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        "name": "DNA", 
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        "name": "DNA Repair", 
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    "datePublished": "1977-10", 
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    "description": "THE excision-repair model for DNA repair involves the incision by an endonuclease of the phosphodiester chain adjacent or close to the damage and subsequent excision by an exonuclease of the defective nucleotide(s) (for review see ref. 1). Specific endonuclease for ultraviolet-induced damage1 and for apurinic sites have been isolated associated with2,3, or without an exonuclease activity (refs 4\u20136 and J.L. and L. Grossman, in preparation). Another class of enzymes does not incise DNA, but recognises and excises defective bases as uracil in the DNA. Belonging to this class of DNA N-glycosidases, is the enzyme described here which excises 3-methyladenine (3-MeAde) from alkylated DNA. This base excision repair is a preparatory step for the nucleotide excision repair describedabove. It has been claimed that endonuclease II of Escherichia coli8 both excises the alkylated bases 3-MeAde and O6-methylguanine (O6-MeGua) and incises DNA atapurinic sites. This enzyme also recognises a number of additional substrates9\u201311. To establish the (precise mechanism of incision of alkylated DNA we have purified two enzymes from Micrococcus luteus, a DNA N-glycosidase, which excises 3-MeAde, and an endonuclease for apurinic sites. We report here a reconstruction experiment showing that incision of DNA treated with carcinogenic and mutagenic compound methyl methanesulphonate (MMS) is a two-step mechanism involving the sequential action of these two enzymes.", 
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        "name": "Nature", 
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    "name": "Two enzymes are required for strand incision in repair of alkylated DNA", 
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