The Mechanism of Dna Repair by Uracil-Dna Glycosylase: Studies Using Nucleotide Analogues

Angelika Rösler Krebs Institute, Departments of Chemistry and Molecular Biology, Sheffield University, Sheffield, S3 7HF

George Panayotou Ludwig Institute for Cancer Research, University College London, London, W1P 8BT

David P. Hornby Krebs Institute, Departments of Chemistry and Molecular Biology, Sheffield University, Sheffield, S3 7HF

Tom Barlow Department of Chemistry, Southampton University, Southampton, S017 1BJ

Tom Brown Department of Chemistry, Southampton University, Southampton, S017 1BJ

Laurence H. Pearl Department of Biochemistry and Molecular Biology, University College London, London, WC1E 6BT

Renos Savva Department of Crystallography, Birkbeck College, University of London, London, WC1E 7HX, UK

G. Michael Blackburn Krebs Institute, Departments of Chemistry and Molecular Biology, Sheffield University, Sheffield, S3 7HF; Department of Chemistry, E-mail: [email protected]

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Abstract

2′,4′-Dideoxy-4′-methyleneuridine incorporated into oligodeoxynucleotides forms regular B-DNA duplexes as shown by T_m 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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The Mechanism of Dna Repair by Uracil-Dna Glycosylase: Studies Using Nucleotide Analogues

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