Gene Review:
UL42 - dsDNA-binding protein
Human herpesvirus 1
- Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis. Randell, J.C., Komazin, G., Jiang, C., Hwang, C.B., Coen, D.M. J. Virol. (2005)
- Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activity. Trego, K.S., Parris, D.S. J. Virol. (2003)
- Cloning, expression, and functional characterization of the equine herpesvirus 1 DNA polymerase and its accessory subunit. Loregian, A., Case, A., Cancellotti, E., Valente, C., Marsden, H.S., Palù, G. J. Virol. (2006)
- The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization. Sherman, G., Gottlieb, J., Challberg, M.D. J. Virol. (1992)
- The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase. Zuccola, H.J., Filman, D.J., Coen, D.M., Hogle, J.M. Mol. Cell (2000)
- Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface. Digard, P., Williams, K.P., Hensley, P., Brooks, I.S., Dahl, C.E., Coen, D.M. Proc. Natl. Acad. Sci. U.S.A. (1995)
- Herpes simplex virus type 1 gene products required for DNA replication: identification and overexpression. Olivo, P.D., Nelson, N.J., Challberg, M.D. J. Virol. (1989)
- The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA. Trego, K.S., Zhu, Y., Parris, D.S. Nucleic Acids Res. (2005)
- Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site. Gibbs, J.S., Weisshart, K., Digard, P., deBruynKops, A., Knipe, D.M., Coen, D.M. Mol. Cell. Biol. (1991)
- The herpes simplex virus type 1 DNA polymerase processivity factor increases fidelity without altering pre-steady-state rate constants for polymerization or excision. Chaudhuri, M., Song, L., Parris, D.S. J. Biol. Chem. (2003)
- Functional interaction between the herpes simplex-1 DNA polymerase and UL42 protein. Hernandez, T.R., Lehman, I.R. J. Biol. Chem. (1990)
- A novel functional domain of an alpha-like DNA polymerase. The binding site on the herpes simplex virus polymerase for the viral UL42 protein. Digard, P., Coen, D.M. J. Biol. Chem. (1990)
- Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype. Johnson, P.A., Best, M.G., Friedmann, T., Parris, D.S. J. Virol. (1991)
- The herpes simplex virus processivity factor, UL42, binds DNA as a monomer. Randell, J.C., Coen, D.M. J. Mol. Biol. (2004)
- DNA and protein interactions of the small subunit of herpes simplex virus type 1 DNA polymerase. Franz, C., Kühn, F.J., Knopf, C.W. Virology (1999)
- A HSV-1 variant (1720) generates four equimolar isomers despite a 9200-bp deletion from TRL and sequences between 9200 np and 97,000 np in inverted orientation being covalently bound to sequences 94,000-126,372 np. Harland, J., Brown, S.M. Virus Genes (1992)
- Rep-dependent initiation of adeno-associated virus type 2 DNA replication by a herpes simplex virus type 1 replication complex in a reconstituted system. Ward, P., Falkenberg, M., Elias, P., Weitzman, M., Linden, R.M. J. Virol. (2001)
- Evaluation of a new general primer pair for rapid detection and differentiation of HSV-1, HSV-2, and VZV by polymerase chain reaction. Baron, J.M., Rübben, A., Grussendorf-Conen, E.I. J. Med. Virol. (1996)
- Interaction between the herpes simplex virus type 1 origin-binding and DNA polymerase accessory proteins. Monahan, S.J., Grinstead, L.A., Olivieri, W., Parris, D.S. Virology (1998)
- Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches. Bridges, K.G., Chow, C.S., Coen, D.M. J. Virol. (2001)
- Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domain. Tenney, D.J., Hurlburt, W.W., Bifano, M., Stevens, J.T., Micheletti, P.A., Hamatake, R.K., Cordingley, M.G. J. Virol. (1993)
- Role of the carboxy terminus of herpes simplex virus type 1 DNA polymerase in its interaction with UL42. Marsden, H.S., Murphy, M., McVey, G.L., MacEachran, K.A., Owsianka, A.M., Stow, N.D. J. Gen. Virol. (1994)