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Uracil excision by bacterial UDG and human hUNG2 is reduced at uracils positioned directly 5' or 3' of a G-quadruplex DNA structures.
The UNG1-PRDX3 (zeige PRDX3 Proteine) interaction protected UNG1 from reactive oxygen species-mediated degradation and prevented mitochondrial DNA oxidation.
Data indicate that DNA glycosylases MYH (zeige MUTYH Proteine), UNG2 (zeige CCNO Proteine), MPG (zeige MPG Proteine), NTH1, NEIL1 (zeige NEIL1 Proteine), 2 and 3 on nascent DNA.
Although the N-terminal domain has minimal effects on DNA binding and uracil excision kinetics, this study reports that this domain enhances the ability of human UNG2 (zeige CCNO Proteine) to translocate on DNA chains as compared to the catalytic domain alone.
Over-expression of uracil DNA glycosylase 2 in HepG2 protect cells against oxidative stress damage.
Results suggest that the UNG2 N-terminus may serve as a flexible scaffold to tether PCNA and RPA at the replication fork, and that post-translational modifications on the UNG2 N-terminus disrupt formation of the PCNA-UNG2-RPA protein complex.
HIV-1 vpr reprograms CRL4(DCAF1) E3 to direct HLTF (zeige HLTF Proteine) for proteasome-dependent degradation independent from previously reported Vpr interactions with base excision repair enzyme uracil DNA glycosylase (UNG2) and crossover junction endonuclease MUS81 (zeige MUS81 Proteine), which Vpr also directs for degradation via CRL4(DCAF1) E3.
Uracil DNA glycosylase (UNG) is the primary glycosylase responsible for the removal of uracils adjacent to cisplatin ICLs, whereas other uracil glycosylases can process uracils in the context of undamaged DNA.
find that the energetic nature of the observed binding free energies of human 8-oxoguanine DNA glycosylase (hOGG1) and human uracil DNA glycosylase (hUNG) for undamaged DNA are derived from different sources. Although hOGG1 uses primarily nonelectrostatic binding interactions with nonspecific DNA, hUNG uses a salt-dependent electrostatic binding mode
The authors show that Vpr can form a trimolecular complex with UNG2 (zeige CCNO Proteine) and RPA32 (zeige RPA2 Proteine) and the positive effect of UNG2 (zeige CCNO Proteine) and RPA32 (zeige RPA2 Proteine) on the reverse transcription process leading to optimal virus replication and dissemination between the primary target cells of HIV-1.
These results together suggest that Unga is implicated in postfertilization genomic DNA demethylation, zygotic gene transcription, and normal embryonic development in zebrafish.
Pms2 (zeige PMS2 Proteine)/Mlh1 (zeige MLH1 Proteine) and multiple uracil glycosylases act jointly, each one with a distinct strand bias, to enlarge the immunoglobulin gene mutation spectrum from G-C to A-T bases.
UNG deficiency reduces B cell clonal expansion in the germinal center in mice and blocks the proliferation of tumor B cells expressing AID.
UNG might be involved in Tet-mediated DNA demethylation.
Study showed elevated levels of homocysteine via dietary folic acid deficiency and chronic hypoperfusion negatively affect learning in Ung deficient mice, while increasing GFAP (zeige GFAP Proteine) immunoreactivity within the dentate gyrus of the hippocampus
Ung and Pms2 (zeige PMS2 Proteine) may exert a mutual backup function for the DNA incision that promotes synthesis by Poleta, each with a distinct strand bias.
transcription factor E2A binds to the UNG2 promoter and represses UNG2 expression.
Differential regulation of S-region hypermutation and class-switch recombination by noncanonical functions of uracil DNA glycosylase.
Our results uncover a specific need for UNG in class-switch recombination for timely and efficient acute Ab responses in vivo
Compared with WT mice, UNG deficiency caused elevated frequency of C:G mutations, suggesting that UNG-mediated U excision led to error-free as well as error-prone repair.
we show that AID binds cooperatively with UNG and the mismatch repair proteins Msh2-Msh6 to Ig Smu and Sgamma3 regions
The crystal structure of D4 in complex with DNA is presented. D4 is a uracil-DNA glycosylase.
description of crystal structure of uracil-DNA glycosylase; several distinctive features revealed
Both uracil DNA glycosylase and deoxyuridine triphosphatase (zeige DUT Proteine) activities are required for full virulence in mice.
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.
, uracil-DNA glycosylase 1, uracil-DNA glycosylase 2
, uracil-DNA glycosylase nuclear isoform