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The mechanism of DNA repair by uracil-DNA glycosylase: Studies using nucleotide analogues

Rosler, A., Panayotou, G., Hornby, D. P., Barlow, T., Brown, T., Pearl, L. H., Savva, R. and Blackburn, G. M. (2000) The mechanism of DNA repair by uracil-DNA glycosylase: Studies using nucleotide analogues Nucleosides Nucleotides and Nucleic Acids, 19, (10-12), pp. 1505-1516.

Record type: Article

Abstract

2',4'-Dideoxy-4'-methyleneuridine incorporated into oligodeoxynucleotides forms regular B-DNA duplexes as shown by Tm and CD measurements. Such oligomers are not cleaved by the DNA repair enzyme, UDG, which cleaves the glycosylic bond in dU but not in dT nor in dC nucleosides in single stranded and double stranded DNA. Differential binding of oligomers containing carbadU, 4'-thiodU, and dU residues to wild type and mutant UDG proteins identify an essential role for the furanose 4'-oxygen in recognition and cleavage of dU residues in DNA.

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More information

Published date: 2000
Keywords: escherichia-coli, cytosine residues, structural basis, excision, catalysis, cyclopentane, glycosidase, deamination, nucleosides, inhibitor

Identifiers

Local EPrints ID: 18977
URI: http://eprints.soton.ac.uk/id/eprint/18977
PURE UUID: 0fe2dad2-3fff-46ad-a119-7404eab1725f

Catalogue record

Date deposited: 18 Jan 2006
Last modified: 17 Jul 2017 16:34

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Contributors

Author: A. Rosler
Author: G. Panayotou
Author: D. P. Hornby
Author: T. Barlow
Author: T. Brown
Author: L. H. Pearl
Author: R. Savva
Author: G. M. Blackburn

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