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Gene Review

UL52  -  helicase-primase primase subunit

Human herpesvirus 1

 
 
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Disease relevance of UL52

 

High impact information on UL52

  • 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 [2].
  • The herpes simplex virus type-1 DNA helicase-primase is a heterotrimer encoded by the UL5, UL8, and UL52 genes [5].
  • These data suggest that the UL52 zinc finger motif plays an important role in the activities of the helicase-primase complex [6].
  • We have developed a panel of 14 monoclonal antibodies (MAbs) to POL, the catalytic subunit of herpes simplex virus type 1 (HSV-1) DNA polymerase encoded by gene UL30, and one MAb to the UL52 protein, another of the seven proteins essential for replication of HSV DNA [7].
  • In contrast, UL52 protein was transported to the nucleus in BHK cells infected with wild-type HSV-1 or with 2-2, a mutant lacking a functional UL9 protein [7].
 

Anatomical context of UL52

  • The failure of the UL52 protein to be correctly transported to the nucleus was also observed in both HFL and Vero cells infected with ambUL8 [7].
 

Physical interactions of UL52

  • Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex [6].
 

Regulatory relationships of UL52

  • The herpes simplex virus type 1 UL8 protein influences the intracellular localization of the UL52 but not the ICP8 or POL replication proteins in virus-infected cells [7].
 

Other interactions of UL52

  • The heterotrimeric helicase-primase complex, encoded by the UL5, UL8 and UL52 genes, is believed to unwind duplex viral DNA at replication forks and to prime lagging strand synthesis [8].
 

Analytical, diagnostic and therapeutic context of UL52

References

  1. Structures of herpes simplex virus type 1 genes required for replication of virus DNA. McGeoch, D.J., Dalrymple, M.A., Dolan, A., McNab, D., Perry, L.J., Taylor, P., Challberg, M.D. J. Virol. (1988) [Pubmed]
  2. 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]
  3. An intertypic herpes simplex virus helicase-primase complex associated with a defect in neurovirulence has reduced primase activity. Barrera, I., Bloom, D., Challberg, M. J. Virol. (1998) [Pubmed]
  4. Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity. Klinedinst, D.K., Challberg, M.D. J. Virol. (1994) [Pubmed]
  5. 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]
  6. Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex. Chen, Y., Carrington-Lawrence, S.D., Bai, P., Weller, S.K. J. Virol. (2005) [Pubmed]
  7. The herpes simplex virus type 1 UL8 protein influences the intracellular localization of the UL52 but not the ICP8 or POL replication proteins in virus-infected cells. Marsden, H.S., Cross, A.M., Francis, G.J., Patel, A.H., MacEachran, K., Murphy, M., McVey, G., Haydon, D., Abbotts, A., Stow, N.D. J. Gen. Virol. (1996) [Pubmed]
  8. The two helicases of herpes simplex virus type 1 (HSV-1). Chattopadhyay, S., Chen, Y., Weller, S.K. Front. Biosci. (2006) [Pubmed]
  9. Deletion mutants of the herpes simplex virus type 1 UL8 protein: effect on DNA synthesis and ability to interact with and influence the intracellular localization of the UL5 and UL52 proteins. Barnard, E.C., Brown, G., Stow, N.D. Virology (1997) [Pubmed]
 
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