Association of origin binding protein and single strand DNA-binding protein, ICP8, during herpes simplex virus type 1 DNA replication in vivo

• Published in: The Journal of biological chemistry 1994-11, Vol.269 (46), p.29329-29334
• Main Authors: Boehmer, P E, Craigie, M C, Stow, N D, Lehman, I R
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Cells, Cultured; DNA Replication; DNA, Viral - biosynthesis; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; herpes simplex virus; Herpesvirus 1, Human - genetics; Molecular Sequence Data; Mutation; Replication Origin; Spodoptera; United States; Viral Proteins - genetics; Viral Proteins - metabolism
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(19)62048-X

The herpes simplex virus type 1 (HSV-1) origin binding protein (UL9 protein) interacts specifically with the HSV-1 encoded single strand DNA-binding protein ICP8 (Boehmer, P.E. and Lehman, I.R. (1994) Proc. Natl. Acad. Sci. U.S.A. 90, 8444-8448). A UL9 mutant protein (UL9DM27) that lacks the C-terminal 27 amino acids shows normal origin-specific DNA binding and retains its DNA-dependent ATPase and helicase activities, but has a greatly reduced affinity for ICP8. The extreme C-terminal portion of the UL9 protein is therefore required for ICP8 binding. The helicase activity of the UL9DM27 protein is approximately 8-fold greater than that of the wild type UL9 protein and is not stimulated by ICP8. The UL9DM27 protein has a reduced ability to replicate origin-containing plasmids in vivo. Consequently, the interaction between the UL9 protein and ICP8 is likely to be important for origin-dependent DNA replication in vivo, presumably to promote efficient unwinding of the DNA at an HSV-1 origin of DNA replication.