A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase

@article{Gallinari1996ANC,
  title={A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase},
  author={Paola Gallinari and Josef Jiricny},
  journal={Nature},
  year={1996},
  volume={383},
  pages={735-738}
}
MISPAIRS in DNA of guanine with uracil and thymine can arise as a result of deamination of cytosine and 5-methylcytosine, respectively. In humans such mispairs are removed by thymine-DNA glycosylase (TDG)1–3. By deleting the carboxy and amino termini of this enzyme we have identified a core region capable of processing G/U but not G/T mispairs. We have further identified two bacterial proteins with strong sequence homology to this core and shown that the homologue from Escherichia coli (dsUDG… 
A novel uracil-DNA glycosylase family related to the helix-hairpin-helix DNA glycosylase superfamily.
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It is reported that MjUDG belongs to a novel UDG family that has not been described to date and has a helix-hairpin-helix motif and a [4Fe-4S]-binding cluster that is considered to be important for the DNA binding and catalytic activity.
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Structure and function in the uracil-DNA glycosylase superfamily.
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Deamination of cytosine to uracil is one of the major pro-mutagenic events in DNA, causing G:C-->A:T transition mutations if not repaired before replication. Repair of uracil-DNA is achieved in a
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Findings suggest that the T. maritima UDG gene has a low level of homology to the E. coli G-T/U mismatch-specific DNA glycosylase gene (mug), and is a member of a new class of DNA repair enzymes.
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This comparison of different substrates under single turnover conditions provides a rational basis for comparing substrates of MUG and relates these conclusions to the known crystal structures of the enzyme and its catalytic mechanism.
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TLDR
This article reviews all developments in view of possible biological functions of this multifaceted DNA glycosylase, which appears to be critically important in developmental processes.
Identification of Escherichia coli Mismatch-specific Uracil DNA Glycosylase as a Robust Xanthine DNA Glycosylase*
TLDR
Molecular modeling and molecular dynamics simulations reveal distinct hydrogen-bonding patterns in the active site of E. coli MUG that account for the specificity differences between MUG and human thymine DNA glycosylase as well as that between the wild type MUGand the Asn-140 and Ser-23 mutants.
A unique uracil-DNA binding protein of the uracil DNA glycosylase superfamily
TLDR
A novel UDG, UdgX, is reported from Mycobacterium smegmatis and other organisms, which specifically recognizes uracil in DNA, forms a tight complex stable to sodium dodecyl sulphate, 2-mercaptoethanol, urea and heat treatment, and shows no detectable Uracil excision.
Repair of deaminated base damage by Schizosaccharomyces pombe thymine DNA glycosylase.
TLDR
This work investigates the DNA repair activity of Spo TDG on all four deaminated bases: xanthine and oxanine (O) from guanine, hypoxanthine (I) from adenine, and uracil from cytosine.
Thymine DNA glycosylase.
TLDR
The objective of this chapter is to put together the results of different lines of experimentation that have explored the thymine DNA glycosylase since its discovery and to critically evaluate their implications for possible physiological roles of this enzyme.
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The characterization of uracil glycosylase activity that can remove the base solely from a mispair with guanine is reported, and it is proposed that its biological role in vivo may also include the correction of a subset of G.T mispairs inefficiently removed by the more abundant ubiquitous uracicil Glycosylases, such as those arising from cytosine deamination in G+C-rich regions of the genome.
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