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Human Uracil-DNA Glycosylase

Gene Structure, Regulation, and Structural Basis for Catalysis

  • Chapter
Advances in DNA Damage and Repair

Part of the book series: NATO ASI Series ((NSSA,volume 302))

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Abstract

Uracil in DNA results from either misincorporation of dUMP residues during replication, or from deamination of cytosine residues. 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 13.8 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 cell. The crystal structure of the catalytic domain of UNG in complex with target DNA has demonstrated that all essential contacts are with the uracil-containing strand. The structure also reveals the mechanism of enzyme-assisted flipping of the uracil-containing nucleotide into the deep catalytic pocket that specifically binds uracil. Nuclear (UNG2) and mitochondrial (UNG1) forms of the enzyme result from the use of two promoters, PA and PB, and alternative splicing. mRNA for UNG1 encodes 304 amino acids, the first 35 of which are unique to this form. mRNA for UNG2 encodes 313 amino acids, the first 44 of which are unique to UNG2. The unique N-terminal sequences in UNG1 and UNG2 are required for mitochondrial and nuclear sorting, respectively, but not for catalytic activity. The 269 amino acid residues common to the two forms include the compact catalytic domain of approximately 220 C-terminal residues and an N-terminal part that binds replication protein A (RPA), indicating a possible role for RPA in base excision repair.

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Authors and Affiliations

  1. UNIGEN Center for Molecular Biology, Norwegian University of Science and Technology, The Medical Faculty, N-7005, Trondheim, Norway

    Hans E. Krokan, Frank Skorpen, Marit Otterlei, Sangeeta Bharati, Kristin Steinsbekk, Hilde Nilsen, Camilla Skjelbred, Bodil Kavli, Rune Standal & Geir Slupphaug

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  1. Hans E. Krokan
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  1. National Institute of Standards and Technology, Gaithersburg, Maryland, USA

    Miral Dizdaroglu

  2. Gazi University, Ankara, Turkey

    Ali Esat Karakaya

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Krokan, H.E. et al. (1999). Human Uracil-DNA Glycosylase. In: Dizdaroglu, M., Karakaya, A.E. (eds) Advances in DNA Damage and Repair. NATO ASI Series, vol 302. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4865-2_18

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