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Thursday, July 30, 2020 | History

2 edition of Escherichia coli uracil-DNA glycosylase found in the catalog.

Escherichia coli uracil-DNA glycosylase

Mary Jane N. Shroyer

Escherichia coli uracil-DNA glycosylase

DNA binding, catalysis, and mechanism of action

by Mary Jane N. Shroyer

  • 19 Want to read
  • 34 Currently reading

Published .
Written in English

    Subjects:
  • Escherichia coli -- Genetics.,
  • Uracil.,
  • DNA-protein interactions.

  • Edition Notes

    Statementby Mary Jane N. Shroyer.
    The Physical Object
    Pagination186 leaves, bound :
    Number of Pages186
    ID Numbers
    Open LibraryOL18138347M

    The Uracil Glycosylase Inhibitor (UGI) of Bacillus subtilis bacteriophage PBS1 is a small protein ( kDa) which inhibits E. coli uracil-DNA glycosylase (UDG) as well as UDG from other species. Inhibition of UDG occurs by reversible protein binding with a UGD:UGI stoichiometry. UGI is capable of dissociating UDG-DNA complexes. Unit definition: One unit Uracil-DNA Glycosylase, heat-labile, is defined as the amount of enzyme required to completely degrade 1 μg purified single-stranded uracil-containing DNA (bacteriophage M13, grown in CJ dut-ung-) at +37°C within 60 minutes. For comparison, one Lindahl unit is comparable to , units based on our unit.

    @article{osti_, title = {Chloroethyinitrosourea-derived ethano cytosine and adenine adducts are substrates for escherichia coli glycosylases excising analogous etheno adducts}, author = {Guliaev, Anton B and Singer, B and Hang, Bo}, abstractNote = {Exocyclic ethano DNA adducts are saturated etheno ring derivatives formed mainly by therapeutic chloroethylnitrosoureas (CNUs), which are. E. coli Uracil N-Glycosylase (UNG)/Buffer Summary. UNG (Uracil DNA N-Glycosylase) is one of four known human DNA N-glycosylases involved in the removal of uracil from DNA. It is a monofunctional enzyme that initiates base excision repair (BER) by hydrolyzing the N-glycosidic bond between the uracil base and the sugar-phosphate backbone in DNA.

    Escherichia coli Fpg Glycosylase Is Nonrendundant and Required for the Rapid Global Repair of Oxidized Purine and Pyrimidine Damage In Vivo Brandy J. Schalow!, Charmain T. Courcelle and Justin Courcelle Department of Biology, Portland State University, PO Box , Portland, OR , USA. Nitric oxide (NO*) is involved in neurotransmission, inflammation, and many other biological processes. Exposure of cells to NO* leads to DNA damage, including formation of deaminated and oxidized bases. Apurinic/apyrimidinic (AP) endonuclease-deficient cells are sensitive to NO* toxicity, which indicates that base excision repair (BER) intermediates are being by:


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Escherichia coli uracil-DNA glycosylase by Mary Jane N. Shroyer Download PDF EPUB FB2

By analogy to uracil-DNA glycosylase, it seemed possible that an enzyme with the ability to release hypoxanthine from DNA might exist, and we have recently demonstrated the presence of such an activity in E.

coli extracts. Hypoxanthine-DNA glycosylase activity is present at a much lower level than uracil-DNA glycosylase activity in crude cell Cited by: 2. Uracil DNA Glycosylase from Escherichia coli; Synonym: Uracil-DNA glycosylase from Escherichia coli, DGU, HIGM4, UDG, UND, UNG1, UNG15; find Sigma-Aldrich-U MSDS, related peer-reviewed papers, technical documents, similar products & more at Sigma-Aldrich.

The gene for the mismatch-specific uracil DNA glycosylase (MUG) was identified in the Escherichia coli genome as a sequence homolog of the human thymine DNA glycosylase with activity against mismatched uracil base pairs.

Examination of cell extracts led us to detect a previously unknown xanthine DNA glycosylase (XDG) activity in E. glycosylase assays with purified enzymes Cited by: Uracil DNA glycosylase (UDG) cleaves the glycosidic bond of deoxyuridine in DNA using a hydrolytic mechanism, with an overall catalytic rate enhancement of fold over the solution reaction.

The nature of the enzyme−substrate interactions that lead to this large rate enhancement are key to understanding enzymatic DNA repair. Using 1H and heteronuclear NMR spectroscopy, we have. The Bacillus subtilis bacteriophage PBS2 uracil- DNA glycosylase inhibitor (Ugi) protein was charac- terized and shown to form a stable complex with Escherichia coli uracil-DNA glycosylase (Ung).

As de- termined by mass spectrometry, the Ugi protein had a molecular weight of 9,   A mutant uracil DNA glycosylase distinguishes between cytosine and 5-methylcytosine.

Contrasting effects of mutating active site residues, aspartic acid 64 and histidine of Escherichia coli uracil-DNA glycosylase on uracil excision and interaction Escherichia coli uracil-DNA glycosylase book an inhibitor protein.

In molecular biology, the protein family, Uracil-DNA glycosylase (UDG) is an enzyme that reverts mutations in DNA. The most common mutation is the deamination of cytosine to repairs these mutations.

UDG is crucial in DNA repair, without it these mutations may lead to cancer. This entry represents various uracil-DNA glycosylases and related DNA glycosylases (), such as uracil-DNA InterPro: IPR View protein in InterPro IPR UDG_fam1 IPR Ura-DNA_Glyclase_AS IPR Uracil-DNA_glycosylase-like IPR Uracil-DNA_glycosylase-like_sf PANTHER i PTHR PTHR, 1 hit.

Escherichia coli cells containing elevated levels of the DNA repair enzyme uracil-DNA glycosylase (the ung gene product) have been constructed by in vitro recombination methods.

First, λnadB transducing phages were isolated from two E. coli DNA libraries by selection of nicotinate-independent lysogens. λnadB phage from one of the libraries were also ung + and carried the ung-nadB genes on an Cited by: Uracil-DNA glycosylase, also known as UNG or UDG, is an human gene is well researched and orthologs exist ubiquitously among prokaryotes and eukaryotes and even in some DNA viruses.

The first uracil DNA-glycosylase was isolated from Escherichia s: UNG, DGU, HIGM4, HIGM5, UDG, UNG1. Specific mutator effects of ung (Uracil-DNA glycosylase) nutations in Escherichia coli Article (PDF Available) in Journal of Bacteriology (2) September with 42 Reads. ) Effects of mutations at tyrosine 66 and asparagine in the active site pocket of Escherichia coli uracil DNA glycosylase on uracil excision from synthetic DNA oligomers: evidence for the occurrence of long‐range interactions between the enzyme and by: 5.

coli Uracil-DNA Glycosylase (UDG) catalyses the release of free uracil from uracil-containing DNA. UDG efficiently hydrolyzes uracil from single-stranded or double-stranded DNA, but not from oligomers (6 or fewer bases).

Product Source An E. coli strain that carries the UDG gene from E. coli. We have expressed a human recombinant uracil-DNA glycosylase (UNG delta 84) closely resembling the mature form of the human enzyme (UNG, from the UNG gene) in Escherichia coli and purified the.

The structure of native and modified uracil-DNA glycosylase from E. coli in solution was studied by synchrotron small-angle X-ray scattering. The modified enzyme (6His-uracil glycosylase) differs from the native one by the presence of an additional N-terminal meric sequence of amino acid residues, including a block of six His residues.

In contrast to minimal differences in the amino acid Author: A. Timchenko, E. Kubareva, E. Volkov, O. Voronina, V. Lunin, D. Gonchar, S.

The nature of the putative general acid His in the reaction catalyzed by Escherichia coli uracil DNA glycosylase (UDG) was investigated using X-ray crystallography and NMR spectroscopy. The crystal structures of HQ UDG, and its complex with uracil, have been solved at and Å.

Uracil‐DNA glycosylase (UDG), a ubiquitous uracil‐excising enzyme found in bacteria and eukaryotes, is one of the enzymes that repair this kind of DNA damage.

Protein mimicry of DNA from crystal structures of the uracil‐DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil‐DNA glycosylase. Mol. Biol., Cited by: Dvolančana uracil-DNK glikozilaza (ECMug, Dug, dsUDG, dvolančana DNK specifična UDG, dsDNK specifična UDG, UdgB, DNK glikozilaza specifična za G:T/U neusklađenost, UDG) je enzim sa sistematskim imenom uracil-dvolančana DNK dezoksiribohidrolaza (otpuštanje uracila).

Ovaj enzim katalizuje sledeću hemijsku reakciju. specifična hidroliza neusklađene dvolančane DNK i BRENDA: BRENDA entry. Uracil DNA Glycosylase (uracil-N-glycosylase) removes uracil residues from the sugar moiety of single- and double-stranded DNA without destroying the phosphodiester backbone, preventing its use as a hybridization target or as a template for DNA polymerases.

UDG will not remove uracil from THE JOURNAL OF BIOLOGICAL CHEMI~TRY 0 by The American Society for Biochemistry and Molecular Biology, Inc. Vol. 7, Issue of March 5, pp. Printed in U.S.A. Hypoxanthine-DNA Glycosylase from Escherichia coli PARTIAL PURIFICATION AND PROPERTIES* (Received for publication, January 8, ).

Saparbaev M, Laval J. 3, N 4-ethenocytosine, a highly mutagenic adduct, is a primary substrate for Escherichia coli double-stranded uracil-DNA glycosylase and human mismatch-specific thymine-DNA glycosylase.

Proc Natl Acad Sci USA –Cited by: 1.by Escherichia coli uracil DNA glycosylase has been investigated. We show that, compared with a single stranded reference substrate, uracil from the first, second, third and the fourth positions of the loops is excised with highly variable efficiencies of.

The latter process results in premutagenic U:G mispairs that, unless uracil is removed, will cause GC→AT transitions in the subsequent round of replication.

The kb gene for human uracil-DNA glycosylase, UNG, is highly conserved and comprises 7 exons. It encodes more than 98% of the total uracil-DNA glycosylase activity in the by: 5.