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6996 545124 Ensembl ENSG00000139372 n/a UniProt Q13569 n/a RefSeq (mRNA) NM_001008411 NM_003211 NM_001363612 XM_006521630 RefSeq (protein) NP_003202 NP_001350541 n/a Location (UCSC) Chr 12: 103.97 – 103.99 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse G/T mismatch-specific thymine DNA glycosylase is an enzyme that in humans is encoded by the TDG gene. Several bacterial ...
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).
NEIL1 recognizes oxidized pyrimidines, formamidopyrimidines, thymine residues oxidized at the methyl group, and both stereoisomers of thymine glycol. [7] The best substrates for human NEIL1 appear to be the hydantoin lesions, guanidinohydantoin, and spiroiminodihydantoin that are further oxidation products of 8-oxoG. NEIL1 is also capable of ...
5hmU can be cleaved by TDG, single-strand-selective monofunctional uracil-DNA glycosylase 1 , Nei-Like DNA Glycosylase 1 , or methyl-CpG binding protein 4 . AP sites and T:G mismatches are then repaired by base excision repair (BER) enzymes to yield cytosine (Cyt). TET1 is a key enzyme involved in demethylating 5mCpG.
The first downward arrow shows thymine DNA glycosylase (TDG) removing 5-formylcytosine (5fC) from the DNA backbone, leaving an apyrimidinic site. Then AP endonuclease cleaves the 5′ deoxyribose-phosphate in the DNA backbone of a single strand, leaving a 3′ hydroxy end and a 5′ deoxyribose phosphate end (second downward arrow).
MBD4 (methyl-CpG-binding domain protein 4) is a glycosylase employed in an initial step of base excision repair. MBD4 protein binds preferentially to fully methylated CpG sites . [ 28 ] These altered bases arise from the frequent hydrolysis of cytosine to uracil (see image) and hydrolysis of 5-methylcytosine to thymine, producing G:U and G:T ...
For instance, Rad-9 acts as an activator for many vital proteins that are responsible for the base excision repair process. First, Rad-9 interacts with many DNA glycosylases that are responsible for repairing specific nucleotide lesions, e.g. Human NEIL1 DNA glycosylase, thymine DNA glycosylase, 8-oxoguanine DNA glycosylase (OGG1). [11]
Thymine-DNA glycosylase (TDG) recognizes the intermediate bases 5fC and 5caC and excises the glycosidic bond resulting in an apyrimidinic site . In an alternative oxidative deamination pathway, 5hmC can be oxidatively deaminated by activity-induced cytidine deaminase/apolipoprotein B mRNA editing complex (AID/APOBEC) deaminases to form 5 ...