Structural elements required for the cooperative binding of the herpes simplex virus origin binding protein to oriS reside in the N-terminal part of the protein

• Published in: The Journal of biological chemistry Vol. 267; no. 24; pp. 17424 - 17429
• Main Authors: Elias, P, Gustafsson, C M, Hammarsten, O, Stow, N D
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 25.08.1992
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cattle; Chromatography, Gel; Cloning, Molecular; Deoxyribonuclease I; DNA - metabolism; DNA Replication; DNA, Viral - genetics; DNA, Viral - metabolism; DNA-Binding Proteins - genetics; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli - genetics; Genes, Viral; herpes simplex virus; Models, Structural; Molecular Sequence Data; Oligodeoxyribonucleotides; Protein Conformation; Simplexvirus - genetics; Simplexvirus - metabolism; Viral Proteins - genetics; Viral Proteins - isolation & purification; Viral Proteins - metabolism
• DOI: 10.1016/S0021-9258(18)41943-6
• ISSN: 0021-9258

The origin binding protein (OBP) of herpes simplex virus type 1 is required to activate a viral origin of replication in vivo. We have used intact OBP as well as a truncated form of the protein expressed in Escherichia coli to investigate the protein-protein interactions, as well as the protein-DNA interactions involved in the formation of a nucleoprotein complex at a viral origin of replication (oriS) in vitro. The salient findings demonstrate that the N-terminal part of OBP is required for the cooperative binding of OBP to three sites (boxes I, II, and III) within oriS. A detailed model for the interaction of OBP with the viral origins of replication oriS and oriL is presented.