Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.

P E Boehmer; I R Lehman

doi:10.1073/pnas.90.18.8444

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Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.

P E Boehmer·I R Lehman

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Abstract

We had previously demonstrated that the herpes simplex virus 1 (HSV-1) single-stranded DNA-binding protein (ICP8) can specifically stimulate the helicase activity of the HSV-1 origin-binding protein (UL9). We show here that this functional stimulation is a manifestation of a tight interaction between UL9 protein and ICP8. By using protein-affinity chromatography, we have demonstrated the specific binding of purified UL9 protein to immobilized ICP8 and vice versa. Furthermore, ICP8 is specifically retained by a column on which the C-terminal 37-kDa DNA-binding domain of the UL9 protein was immobilized. The interaction between ICP8 and the DNA-binding domain of the UL9 protein was confirmed by cochromatography of the two proteins. These results suggest that the UL9 protein and ICP8 form a tight complex that functions in origin recognition and unwinding.

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Animals Baculoviridae Binding Sites Chromatography, Affinity DNA-Binding Proteins Genetic Vectors Moths Simplexvirus Transfection Viral Proteins Journal Article Research Support, U.S. Gov't, P.H.S.

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P E Boehmer, I R Lehman. 1993-09-15. Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.. https://doi.org/10.1073/pnas.90.18.8444

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