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Literature summary for 2.1.1.37 extracted from

  • Boland, M.J.; Christman, J.K.
    Characterization of Dnmt3b:thymine-DNA glycosylase interaction and stimulation of thymine glycosylase-mediated repair by DNA methyltransferase(s) and RNA (2008), J. Mol. Biol., 379, 492-504.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.37

Cloned(Commentary)

Cloned (Comment) Organism
co-expression of Dnmt3b with Tdg or Mbd4 in HEK293T cells Mus musculus

Protein Variants

Protein Variants Comment Organism
A609T naturally occuring mutation causing recessive genetic disorder, ICF syndrome, the mutation does not affect the association of Dnmt3b with Mbd4 or Tdg Mus musculus
additional information construction of several Xpress-tagged Dnmt3b C-terminal truncation mutants, Dnmt3b mutants possessing the conserved MTase motifs VI, IV or I are all capable of binding Tdg, while removal of the entire catalytic domain of Dnmt3b disrupts its interaction with Tdg. Deletion of both putative interaction regions, PWWP and I, from Dnmt3b eliminates the binding ability. Reduction of T·G mismatch repair efficiency upon loss of DNA methyltransferase expression Mus musculus
S277P naturally occuring mutation causing recessive genetic disorder, ICF syndrome, the mutation does not affect the association of Dnmt3b with Mbd4 or Tdg Mus musculus
V612A naturally occuring mutation causing recessive genetic disorder, ICF syndrome, the mutation does not affect the association of Dnmt3b with Mbd4 or Tdg Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
heterochromatin both Tdg and Dnmt3b are colocalized to heterochromatin Mus musculus 792
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nucleus
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 Mus musculus 5634
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus interactions between Dnmt3b and both Tdg and Mbd4, i.e. G/T mismatch-specific thymine-DNA glycosylase and methyl-CpG binding domain protein 4, two thymine glycosylases involved in reduction of the impact of 5mC deamination, that can both excise uracil or thymine at U-G and T-G mismatches to initiate base excision repair, overview. Interaction with Tdg via two separate Dnmt3b domains, but MTase motif I of the catalytic domain of Dnmt3b is sufficient for interaction with Tdg and Mbd4 ?
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 ?

Organism

Organism UniProt Comment Textmining
Mus musculus O88509
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Source Tissue

Source Tissue Comment Organism Textmining
embryonic stem cell
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 Mus musculus
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F9 embryonal carcinoma cell an asynchronously proliferating population of carcinoma cells Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information interactions between Dnmt3b and both Tdg and Mbd4, i.e. G/T mismatch-specific thymine-DNA glycosylase and methyl-CpG binding domain protein 4, two thymine glycosylases involved in reduction of the impact of 5mC deamination, that can both excise uracil or thymine at U-G and T-G mismatches to initiate base excision repair, overview. Interaction with Tdg via two separate Dnmt3b domains, but MTase motif I of the catalytic domain of Dnmt3b is sufficient for interaction with Tdg and Mbd4 Mus musculus ?
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 ?

Subunits

Subunits Comment Organism
More Dnmt3b is composed of multiple domains. The C-terminus contains the catalytic domain which harbors conserved C-5 DNA methyltransferase motif that are necessary for catalyzing methyl transfer from the cofactor S-adenosyl-L-methionine to the target cytosine. The N-terminus contains a PWWP domain and an ATRX-like domain, so called because it shares homology with the alpha-thalassemia/mental retardation syndrome, X-linked, i.e. ATRX, protein Mus musculus

Synonyms

Synonyms Comment Organism
C5 MTase
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 Mus musculus
DNMT3B
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 Mus musculus