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Gene Review

UL2  -  uracil-DNA glycosylase

Human herpesvirus 1

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Disease relevance of UL2


High impact information on UL2


Biological context of UL2

  • A 28.5 kDa catalytic fragment of the uracil-DNA glycosylase DNA repair enzyme from Herpes simplex virus type 1 (HSV-1) has been crystallized using protein from a highly expressing Escherichia coli clone of the Herpes simplex virus type 1 UL2 gene [5].
  • Viral mutants with lesions in either or both of genes UL2 and UL44, which are not essential for growth in cell culture, were constructed using cosmids containing specifically introduced frameshift mutations [6].
  • Hence, HSV1 uracil-DNA glycosylase, dispensable in viral proliferation in tissue culture, could be essential in neurons for the "cleansing" of the viral genome of uracil residues before the start of replication [7].
  • We conclude that the damage recognition step in the HSV-1 UDG reaction pathway is modulated by local DNA sequence [8].
  • Systematic examination of the kinetics and binding of UDG with these different substrates has enabled us to examine the origin of the sequence preferences [8].

Anatomical context of UL2


Analytical, diagnostic and therapeutic context of UL2


  1. Evidence that the herpes simplex virus type 1 uracil DNA glycosylase is required for efficient viral replication and latency in the murine nervous system. Pyles, R.B., Thompson, R.L. J. Virol. (1994) [Pubmed]
  2. Transcriptional and translational analyses of the UL2 gene of equine herpesvirus 1: a homolog of UL55 of herpes simplex virus type 1 that is maintained in the genome of defective interfering particles. Harty, R.N., Holden, V.R., O'Callaghan, D.J. J. Virol. (1993) [Pubmed]
  3. Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex. Savva, R., Pearl, L.H. Nat. Struct. Biol. (1995) [Pubmed]
  4. Herpes simplex virus type 1 uracil-DNA glycosylase: isolation and selective inhibition by novel uracil derivatives. Focher, F., Verri, A., Spadari, S., Manservigi, R., Gambino, J., Wright, G.E. Biochem. J. (1993) [Pubmed]
  5. Crystallization and preliminary X-ray analysis of the uracil-DNA glycosylase DNA repair enzyme from herpes simplex virus type 1. Savva, R., Pearl, L.H. J. Mol. Biol. (1993) [Pubmed]
  6. A cosmid-based system for constructing mutants of herpes simplex virus type 1. Cunningham, C., Davison, A.J. Virology (1993) [Pubmed]
  7. Uracil in OriS of herpes simplex 1 alters its specific recognition by origin binding protein (OBP): does virus induced uracil-DNA glycosylase play a key role in viral reactivation and replication? Focher, F., Verri, A., Verzeletti, S., Mazzarello, P., Spadari, S. Chromosoma (1992) [Pubmed]
  8. A kinetic analysis of substrate recognition by uracil-DNA glycosylase from herpes simplex virus type 1. Bellamy, S.R., Baldwin, G.S. Nucleic Acids Res. (2001) [Pubmed]
  9. Direct measurement of the substrate preference of uracil-DNA glycosylase. Panayotou, G., Brown, T., Barlow, T., Pearl, L.H., Savva, R. J. Biol. Chem. (1998) [Pubmed]
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