Abstract
Deamination of adenine occurs in DNA, RNA, and their precursors via a hydrolytic reaction and a nitrosative reaction. The generated deaminated products are potentially mutagenic because of their structural similarity to natural bases, which in turn leads to erroneous nucleotide pairing and subsequent disruption of cellular metabolism. Incorporation of deaminated precursors into the nucleic acid strand occurs during nucleotide synthesis by DNA and RNA polymerases or base modification by DNA- and/or RNA-editing enzymes during cellular functions. In such cases, removal of deaminated products from DNA and RNA by a nuclease might be required depending on the cellular function. One such enzyme, endonuclease V, recognizes deoxyinosine and cleaves 3' end of the damaged base in double-stranded DNA through an alternative excision repair mechanism in Escherichia coli, whereas in Homo sapiens, it recognizes and cleaves inosine in single-stranded RNA. However, to explore the role of endonuclease V in vivo, a detailed analysis of cell biology is required. Based on recent reports and developments on endonuclease V, we discuss the potential functions of endonuclease V in DNA repair and RNA metabolism.
Highlights
Genomic DNA is supposed to contain error-free genetic information to facilitate the proper functioning of the cell, it is prone to damage, deterioration, and modifications due to environmental and endogenous factors
Irradiation or genotoxic chemicals, and base excision repair (BER), which is used for non-bulky and non-helix-distorting DNA modifications induced by alkylation, oxidation, and deamination
The cytosine deamination product deoxyuridine is a nucleoside with uracil attached to the deoxyribose ring; this deamination product is subjected to BER, initiated by a monofunctional uracil-DNA glycosylase
Summary
Genomic DNA is supposed to contain error-free genetic information to facilitate the proper functioning of the cell, it is prone to damage, deterioration, and modifications due to environmental and endogenous factors. The cytosine deamination product deoxyuridine is a nucleoside with uracil attached to the deoxyribose ring; this deamination product is subjected to BER, initiated by a monofunctional uracil-DNA glycosylase This enzyme searches the genome to locate sites of damage and catalyzes the hydrolysis of the N-glycosidic bond to release the lesion and generate an apurinic/apyrimidinic (AP) site. A recent report has shown that hEndoV localizes to the cytoplasm, preferentially binds to RNA, and cleaves the single-strand region containing inosine, which was generated by RNA-editing enzymes [12,13] These data suggest the possibility that hEndoV controls the fate of inosine-containing RNA in humans, its function as a DNA repair enzyme cannot be ruled out [14]
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