Linked Life Data

2193033

Source:http://linkedlifedata.com/resource/pubmed/id/2193033

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pubmed-article:2193033pubmed:abstractTextThe herpes simplex virus 1 (HSV-1) UL42 protein, one of seven herpes-encoded polypeptides that are required for the replication of the HSV-1 genome, is found in a 1:1 complex with the HSV-1 DNA polymerase (Crute, J. J., and Lehman, I. R. (1989) J. Biol. Chem. 264, 19266-19270). To obtain herpes DNA polymerase free of UL42 protein, we have cloned and overexpressed the Pol gene in a recombinant baculovirus vector and purified the recombinant DNA polymerase to near homogeneity. Replication of singly primed M13mp18 single-stranded DNA by the recombinant enzyme in the presence of the herpes encoded single-stranded DNA-binding protein ICP8 yields in addition to some full-length product a distribution of intermediate length products by a quasi-processive mode of deoxynucleotide polymerization. Addition of the purified UL42 protein results in completely processive polymerization and the generation of full-length products. Similar processivity is observed with the HSV-1 DNA polymerase purified from herpes-infected Vero cells. Processive DNA replication by the DNA polymerase isolated from HSV-1-infected Vero cells or the recombinant DNA polymerase-UL42 protein complex requires that the single-stranded DNA be coated with saturating levels of ICP8. ICP8 which binds single-stranded DNA in a highly cooperative manner is presumably required to melt out regions of secondary structure in the single-stranded DNA template, thereby potentiating the processivity enhancing action of the UL42 protein.lld:pubmed
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pubmed-article:2193033pubmed:articleTitleFunctional interaction between the herpes simplex-1 DNA polymerase and UL42 protein.lld:pubmed
pubmed-article:2193033pubmed:affiliationDepartment of Biochemistry, Beckman Center, Stanford University School of Medicine, California 94305-5307.lld:pubmed
pubmed-article:2193033pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2193033pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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