The herpes simplex virus type-1 origin binding protein: DNA helicase activity

P. E. Boehmer, M. S. Dodson, I. R. Lehman

Research output: Contribution to journalArticlepeer-review

79 Scopus citations


The herpes simplex virus type 1 (HSV-1) origin binding protein, the product of the UL9 gene, catalyzes the unwinding of DNA in the 3′-5′ direction. Helicase activity is coupled to the hydrolysis of ATP or dATP and to a lesser extent to CTP, dCTP, or UTP. It requires a divalent cation (Mg2+ > Mn2+ > Ca2+) with an optimum at 2.5 mM MgCl. Activity is optimal at high pH (8.5-9.5) and high temperature (45°C) and is inhibited at ionic strengths > 50 mM NaCl. The helicase activity is specifically stimulated by the HSV-1-encoded single-stranded DNA-binding protein, ICP8, which increases both the rate and extent of helicase activity. Helicase action appears to be stoichiometric, requiring a DNA-dependent assembly of a multimeric UL9 protein complex. Under optimal conditions, the rate of DNA unwinding is approximately 75 base pairs/min.

Original languageEnglish (US)
Pages (from-to)1220-1225
Number of pages6
JournalJournal of Biological Chemistry
Issue number2
StatePublished - Jan 15 1993

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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