The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

UL5  -  helicase-primase helicase subunit

Human herpesvirus 1

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of UL5

  • The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding [1].
  • Several hypotheses for the role of motif V in the function of the UL5 helicase in HSV-1 DNA replication are considered [2].

High impact information on UL5

  • Photocross-linking experiments with subcomplexes containing mutant versions of UL5 and wild type UL52 indicated that the integrity of the ATP binding region is important for DNA binding of both subunits [1].
  • Herpes simplex virus type 1 encodes a heterotrimeric helicase-primase complex composed of the products of the UL5, UL52, and UL8 genes [1].
  • A gel mobility shift assay indicated that the UL5-UL52 subcomplex binds more efficiently to the forked substrate than to either single strand or duplex DNA [1].
  • Herpes simplex virus type 1 encodes a helicase-primase complex composed of the products of the UL5, UL52, and UL8 genes [2].
  • Although the role of the other four motifs is not known, single amino acid substitutions created in conserved residues in all six motifs abolish the ability of UL5 to support viral DNA replication in vivo (Zhu, L., and Weller, S. K. (1992) J. Virol. 66, 469-479) [2].

Biological context of UL5

  • So far, four HSV-1 early genes, UL5/8/52 (helicase primase complex) and UL29 (single-stranded DNA-binding protein), were defined as sufficient for AAV replication when cells were transfected with a plasmid carrying the wild-type AAV-2 genome [3].
  • In addition, nucleotide sequence analysis showed that the MluI sites not found in the F2 and C7805 types were located in the regions homologous to the herpes simplex virus type 1 gI and UL5 genes, respectively [4].

Associations of UL5 with chemical compounds

  • Although nucleotides are not absolutely required for DNA binding, ADP stimulated the binding of UL5-UL52 to single strand DNA whereas ATP, ADP, and adenosine 5'-O-(thiotriphosphate) stimulated the binding to a forked substrate [1].

Physical interactions of UL5

  • These results are consistent with the proposal that the putative zinc binding motif of UL52 is required not only for binding of the UL52 subunit to DNA and for primase activity but also for optimal binding of UL5 to DNA and for the subsequent ATPase and helicase activities [5].

Other interactions of UL5

  • The nucleoside triphosphatase activity of the UL5/UL52 subassembly is strongly stimulated by both homo- and heteropolymeric single-stranded DNA [6].
  • These data suggest that UL8 protein mediates an interaction between the UL5/52 core enzyme and ICP8 that optimizes the utilization of ICP8-covered DNA templates during DNA replication [7].
  • From the analysis of mutants defective in both UL30 and UL5, we suggest that the prereplicative site pattern can form under conditions in which viral and/or cellular polymerases are inhibited [8].
  • From the analysis of mutants lacking both UL5 and UL9, we conclude that neither viral helicase is required for the prereplicative site pattern to form as long as a polymerase inhibitor is present [8].

Analytical, diagnostic and therapeutic context of UL5


  1. The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding. Biswas, N., Weller, S.K. J. Biol. Chem. (2001) [Pubmed]
  2. Replacement of gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicase-primase. Graves-Woodward, K.L., Weller, S.K. J. Biol. Chem. (1996) [Pubmed]
  3. Herpes simplex virus type 1 ICP0 protein mediates activation of adeno-associated virus type 2 rep gene expression from a latent integrated form. Geoffroy, M.C., Epstein, A.L., Toublanc, E., Moullier, P., Salvetti, A. J. Virol. (2004) [Pubmed]
  4. Restriction endonuclease analysis of field isolates of feline herpesvirus type 1 and identification of heterogeneous regions. Maeda, K., Kawaguchi, Y., Ono, M., Tajima, T., Mikami, T. J. Clin. Microbiol. (1995) [Pubmed]
  5. A mutation in the C-terminal putative Zn2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex. Biswas, N., Weller, S.K. J. Biol. Chem. (1999) [Pubmed]
  6. Interactions of a subassembly of the herpes simplex virus type 1 helicase-primase with DNA. Healy, S., You, X., Dodson, M. J. Biol. Chem. (1997) [Pubmed]
  7. The UL8 subunit of the herpes simplex virus type-1 DNA helicase-primase optimizes utilization of DNA templates covered by the homologous single-strand DNA-binding protein ICP8. Tanguy Le Gac, N., Villani, G., Hoffmann, J.S., Boehmer, P.E. J. Biol. Chem. (1996) [Pubmed]
  8. Herpes simplex virus type 1 prereplicative sites are a heterogeneous population: only a subset are likely to be precursors to replication compartments. Lukonis, C.J., Burkham, J., Weller, S.K. J. Virol. (1997) [Pubmed]
  9. The UL8 subunit of the heterotrimeric herpes simplex virus type 1 helicase-primase is required for the unwinding of single strand DNA-binding protein (ICP8)-coated DNA substrates. Falkenberg, M., Bushnell, D.A., Elias, P., Lehman, I.R. J. Biol. Chem. (1997) [Pubmed]
WikiGenes - Universities