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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 ...
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). [1] [2] [3] This enzyme ...
UNG is known to be the major player in uracil removal but when depleted SMUG1 can provide a backup for UNG in the antibody diversification process. [11] [12] In addition to uracil, SMUG1 removes several pyrimidine oxidation products. [13] and has a specific function to remove the thymine oxidation product 5-hydroxymethyl uracil from DNA. [14]
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 ]
The uracil may be excised by uracil-DNA glycosylase (UNG), resulting in an abasic site. This abasic site (or AP, apurinic/apyrimidinic) may be copied by a translesion synthesis DNA polymerase such as DNA polymerase eta, resulting in random incorporation of any of the four nucleotides, i.e. A, G, C, or T.
This is the most common single nucleotide mutation. In DNA, this reaction, if detected prior to passage of the replication fork, can be corrected by the enzyme thymine-DNA glycosylase, which removes the thymine base in a G/T mismatch. This leaves an abasic site that is repaired by AP endonucleases and polymerase, as with uracil-DNA glycosylase. [2]
Very short patch (VSP) repair is a DNA repair system that removes GT mismatches created by the deamination of 5-methylcytosine to thymine.This system exists because the glycosylases which normally target deaminated bases cannot target thymine (it being one of the regular four bases in DNA).