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The herpes simplex virus type-1 origin binding protein. DNA helicase activity
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+...
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Published in: | The Journal of biological chemistry 1993-01, Vol.268 (2), p.1220-1225 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 degrees 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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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(18)54063-1 |