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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 ...
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 ...
Human MBD4 protein has 580 amino acids with a methyl-CpG-binding domain at amino acids 82–147 and a C-terminal DNA glycosylase domain at amino acids 426–580. [8] These domains are separated by an intervening region that interacts with UHRF1, an E3 ubiquitin ligase, and USP7, a de-ubiquinating enzyme.
Spontaneous deamination of 5-methylcytosine results in thymine and ammonia. 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 ...
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 ...
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 ...
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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]