@article{mbs:/content/journal/jgv/10.1099/0022-1317-76-12-3125, author = "Abbotts, Adrian P. and Stow, Nigel D.", title = "The origin-binding domain of the herpes simplex virus type 1 UL9 protein is not required for DNA helicase activity", journal= "Journal of General Virology", year = "1995", volume = "76", number = "12", pages = "3125-3130", doi = "https://doi.org/10.1099/0022-1317-76-12-3125", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-76-12-3125", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The UL9 protein of herpes simplex virus type 1 binds to specific sequences within the viral origins of DNA replication and also functions as a DNA helicase. The C-terminal 317 amino acids of the 851 residue protein specify sequence-specific binding to the viral origins and the N-terminal 400 contain several motifs characteristic of many DNA and RNA helicases. To investigate whether the origin-binding domain is required for helicase function we have expressed a truncated version comprising amino acids 1-535 of UL9 using a recombinant baculovirus. Extracts were prepared from cells infected with the recombinant virus and chromatographed over ATP-agarose. DNA helicase, DNA-dependent ATPase and a novel single-stranded DNA-binding activity were present in fractions containing the truncated UL9 protein but not in corresponding gradient fractions from a control virus infection. These results indicate that the DNA helicase function of UL9 does not require the presence of the origin-binding domain and suggest that an interaction between the N-terminal domain and distorted or partially single-stranded regions of DNA may play a role in unwinding the origin region.", }