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At least five major DNA repair pathwaysbase excision repair (BER), nucleotide excision repair (NER), mismatch repair (MMR), homologous recombination (HR) and non-homologous end joining (NHEJ)are active throughout different stages of the cell cycle, allowing the cells to repair the DNA damage.
DNA glycosylases play a key role in the elimination of such DNA lesions; they recognize and excise damaged bases, thereby initiating a repair process that restores the regular DNA structure with high accuracy.
DNA glycosylases are a family of enzymes involved in base excision repair, classified under EC number EC 3.2. 2. Base excision repair is the mechanism by which damaged bases in DNA are removed and replaced.
DNA Glycosylases: Mechanisms DNA glycosylases use a remarkable nucleotide-flipping mechanism to extrude damaged nucleotides from the DNA helix, thereby coupling lesion recognition and catalysis. Some glycosylases are specific for a single lesion, while others handle multiple forms of damage.
BER is important for removing damaged bases that could otherwise cause mutations by mispairing or lead to breaks in DNA during replication. BER is initiated by DNA glycosylases, which recognize and remove specific damaged or inappropriate bases, forming AP sites. These are then cleaved by an AP endonuclease.
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Simple Summary. Thymine DNA Glycosylase (TDG) is a DNA repair protein that plays an important role in gene regulation. Recent studies have shown that TDG interacts with various transcription factors to activate target genes.
The UNG1 gene encodes the major uracil-DNA glycosylase (UDG) that excises uracil from DNA. Bacterial, yeast and mouse cells deficient in Ung1 protein (Ung1p) exhibit increased levels of spontaneous mutation frequencies in the nuclear genome (610).

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