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22256 Ensembl ENSG00000076248 ENSMUSG00000029591 UniProt P13051 P97931 RefSeq (mRNA) NM_080911 NM_003362 NM_001040691 NM_011677 RefSeq (protein) NP_003353 NP_550433 NP_001035781 NP_035807 Location (UCSC) Chr 12: 109.1 – 109.11 Mb Chr 5: 114.27 – 114.28 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Uracil-DNA glycosylase (also known as UNG or UDG) is an enzyme. Its most ...
A variety of glycosylases that recognize different types of damage exist, including oxidized or methylated bases, or uracil in DNA. The AP site can then be cleaved by an AP endonuclease, leaving 3'-hydroxyl and deoxyribose-5-phosphate termini (see DNA structure). In alternative fashion, bifunctional glycosylase-lyases can cleave the AP site ...
Uracil DNA glycosylase flips a uracil residue out of the duplex, shown in yellow. DNA glycosylases are responsible for initial recognition of the lesion. They flip the damaged base out of the double helix, as pictured, and cleave the N-glycosidic bond of the damaged base, leaving an AP site. There are two categories of glycosylases ...
Uracil-DNA glycosylases are DNA repair enzymes that excise uracil residues from DNA by cleaving the N-glycosydic bond, initiating the base excision repair pathway. Uracil in DNA can arise either through the deamination of cytosine to form mutagenic U:G mispairs, or through the incorporation of dUMP by DNA polymerase to form U:A pairs . [ 18 ]
NHEJ and heat-labile sites. Induction of heat-labile sites (HLS) is a signature of ionizing radiation. The DNA clustered damage sites consist of different types of DNA lesions. Some of these lesions are not prompt DSBs but they convert to DSB after heating. HLS are not evolved to DSB under physiological temperature (37 C).
Structure of the base-excision repair enzyme uracil-DNA glycosylase excising a hydrolytically-produced uracil residue from DNA. The uracil residue is shown in yellow. When only one of the two strands of a double helix has a defect, the other strand can be used as a template to guide the correction of the damaged strand.
Single-strand selective monofunctional uracil DNA glycosylase is an enzyme that in humans is encoded by the SMUG1 gene. [ 4 ] [ 5 ] [ 6 ] SMUG1 is a glycosylase that removes uracil from single- and double-stranded DNA in nuclear chromatin, thus contributing to base excision repair .
Double-stranded uracil-DNA glycosylase (EC 3.2.2.28, Mug, double-strand uracil-DNA glycosylase, Dug, dsUDG, double-stranded DNA specific UDG, dsDNA specific UDG, UdgB, G:T/U mismatch-specific DNA glycosylase, UDG) is an enzyme with systematic name uracil-double-stranded DNA deoxyribohydrolase (uracil-releasing).