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Uracil-DNA glycosylase

uracil-DNA glycosylase, UNG, UDG, DGU, UNG2
This gene encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2. The UNG2 term was used as a previous symbol for the CCNO gene (GeneID 10309), which has been confused with this gene, in the literature and some databases. [provided by RefSeq, Nov 2010] (from NCBI)
Top mentioned proteins: CAN, POLYMERASE, ACID, HAD, STEP
Papers using uracil-DNA glycosylase antibodies
High-resolution analysis of DNA regulatory elements by synthetic saturation mutagenesis
Caruthers Marvin H. et al., In Nucleic Acids Research, 2008
... Restriction endonucleases (AscI, BstXI, ClaI), T4 polynucleotide kinase (PNK), T4 DNA ligase and Uracil-DNA glycosylase (UDG) were obtained from New England Biolabs Inc ...
Papers on uracil-DNA glycosylase
Transcription Factors and DNA Repair Enzymes Compete for Damaged Promoter Sites.
Strauss et al., United States. In J Biol Chem, Feb 2016
We incubated 39-mer CRE-containing ds oligonucleotides with recombinant CREB1 alone or with UNG2 or OGG1, followed by electrophoretic mobility shift assay (EMSA).
Uracil-DNA Glycosylase UNG Promotes Tet-mediated DNA Demethylation.
Du et al., Shanghai, China. In J Biol Chem, Feb 2016
UNG2, one of the glycosylases known to excise uracil residues from DNA, was found to reduce DNA methylation, thus activating transcription of a methylation-silenced reporter gene when co-transfected with Tet2 into HEK293T cells.
Non-canonical uracil processing in DNA gives rise to double-strand breaks and deletions: relevance to class switch recombination.
Jiricny et al., Zürich, Switzerland. In Nucleic Acids Res, Feb 2016
Although U/G mispairs arising in this way are generally efficiently repaired to C/Gs by uracil DNA glycosylase (UNG)-initiated base excision repair (BER), uracil processing in S-regions of activated B-cells occasionally gives rise to double strand breaks (DSBs), which trigger CSR.
[Cloning, expression, purification and characterization of two uracil-DNA glycosylases from Sulfolobus acidocaldarius].
Liu et al., In Wei Sheng Wu Xue Bao, Sep 2015
OBJECTIVE: To characterize uracil-DNA glycosylase from acidophilic and thermophilic Sulfolobus acidocaldarius.
Uracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes.
Chattopadhyay et al., Birmingham, United States. In Protein Sci, 2014
The UDG superfamily is classified into six families based on their substrate specificity.
Opinion: uracil DNA glycosylase (UNG) plays distinct and non-canonical roles in somatic hypermutation and class switch recombination.
Honjo et al., Kyoto, Japan. In Int Immunol, 2014
Uracil DNA glycosylase (UNG), a member of the base excision repair complex, is required for CSR.
Error-free versus mutagenic processing of genomic uracil--relevance to cancer.
Slupphaug et al., Trondheim, Norway. In Dna Repair (amst), 2014
Nuclear uracil-DNA glycosylase UNG2 is the major enzyme initiating BER of uracil of U:A pairs as well as U:G mismatches.
Human cytidine deaminases facilitate hepatitis B virus evolution and link inflammation and hepatocellular carcinoma.
Cao et al., Shanghai, China. In Cancer Lett, 2014
Their editing efficiency is counteracted by uracil-DNA glycosylase.
Base excision repair.
Bjørås et al., Trondheim, Norway. In Cold Spring Harb Perspect Biol, 2013
More recently, an important role of uracil-DNA glycosylase UNG2 in adaptive immunity was revealed.
Strikingly different properties of uracil-DNA glycosylases UNG2 and SMUG1 may explain divergent roles in processing of genomic uracil.
Kavli et al., Trondheim, Norway. In Dna Repair (amst), 2012
Data show that uracil-DNA glycosylases SMUG1 and UNG2 display widely different sequence preferences.
The UNG2 Arg88Cys variant abrogates RPA-mediated recruitment of UNG2 to single-stranded DNA.
Slupphaug et al., Trondheim, Norway. In Dna Repair (amst), 2012
Data show that the R88C variant impairs binding of the R88C variant impairs binding of uracil-DNA glycosylase UNG2 to replication protein A RPA2.
Ectopic restriction of DNA repair reveals that UNG2 excises AID-induced uracils predominantly or exclusively during G1 phase.
Jolly et al., Sydney, Australia. In J Exp Med, 2012
Excision of AID-induced Uracil by UNG2 occurs predominantly during G1 phase, inducing faithful repair, mutagenic processing, and class switching.
Recruitment of the nuclear form of uracil DNA glycosylase into virus particles participates in the full infectivity of HIV-1.
Benichou et al., Paris, France. In J Virol, 2012
Recruitment of the UNG2 into virus particles increased the infectivity of HIV-1.
The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover.
de Noronha et al., Albany, United States. In Plos One, 2011
Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover.
Embryonic lethal phenotype reveals a function of TDG in maintaining epigenetic stability.
Schär et al., Basel, Switzerland. In Nature, 2011
Thymine DNA glycosylase (TDG) is a member of the uracil DNA glycosylase (UDG) superfamily of DNA repair enzymes.
Uracil residues dependent on the deaminase AID in immunoglobulin gene variable and switch regions.
Gearhart et al., Baltimore, United States. In Nat Immunol, 2011
Here we demonstrate their presence by determining the sensitivity of DNA to digestion with uracil DNA glycosylase (UNG) and abasic endonuclease.
Primary B cell immunodeficiencies: comparisons and contrasts.
Campana et al., Memphis, United States. In Annu Rev Immunol, 2008
Hyper-IgM syndromes result from mutations in CD40 ligand, CD40, AID, or UNG in 70-80% of affected patients.
Mechanism and regulation of class switch recombination.
Schrader et al., Worcester, United States. In Annu Rev Immunol, 2007
AID activity converts several dC bases to dU bases in each S region, and the dU bases are then excised by the uracil DNA glycosylase UNG; the resulting abasic sites are nicked by apurinic/apyrimidinic endonuclease (APE).
Enzymatic capture of an extrahelical thymine in the search for uracil in DNA.
Stivers et al., Baltimore, United States. In Nature, 2007
for the human and Escherichia coli UNG enzymes, discrimination of thymine and uracil is initiated by thermally induced opening of T*A and U*A base pairs and not by active participation of the enzyme
Site-Specific Mutagenesis in Escherichia coli by Bulky Exocyclic Amino-Substituted Guanine and Adenine Derivatives in Double-Stranded or Gapped Plasmids.
Moon, In Cancer Res Treat, 2003
The uracil residues lead to the creation of a gap in the complementary strand due to the actions of E. coli uracil-DNA glycosylase and AP endonuclease.
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