TY - JOUR
T1 - The herpes simplex virus type-1 origin binding protein. DNA helicase activity
AU - Boehmer, P. E.
AU - Dodson, M. S.
AU - Lehman, I. R.
PY - 1993
Y1 - 1993
N2 - 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 MgCl2. 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.
AB - 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 MgCl2. 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.
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M3 - Article
C2 - 8380408
AN - SCOPUS:0027392690
VL - 268
SP - 1220
EP - 1225
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 2
ER -