In vitro strand exchange promoted by the herpes simplex virus type-1 single strand DNA-binding protein (ICP8) and DNA helicase-primase

Amitabh V. Nimonkar, Paul E Boehmer

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

The genome of herpes simplex virus type-1 undergoes a high frequency of homologous recombination in the absence of a virus-encoded RecA-type protein. We hypothesized that viral homologous recombination is mediated by the combined action of the viral single strand DNA-binding protein (ICP8) and helicase-primase. Our results show that ICP8 catalyzes the formation of recombination intermediates (joint molecules) between circular single-stranded acceptor and linear duplex donor DNA. Joint molecules formed by invasion of a 3′-terminal strand displaces the non-complementary 5′-terminal strand, thereby creating a loading site for the helicase-primase. Helicase-primase acts on these joint molecules to promote ATP-dependent branch migration. Finally, we have reconstituted strand exchange by the synchronous action of ICP8 and helicase-primase. Based on these data, we present a recombination mechanism for a eukaryotic DNA virus in which a single strand DNA-binding protein and helicase cooperate to promote homologous pairing and branch migration.

Original languageEnglish (US)
Pages (from-to)15182-15189
Number of pages8
JournalJournal of Biological Chemistry
Volume277
Issue number17
DOIs
StatePublished - Apr 26 2002
Externally publishedYes

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DNA Primase
DNA Helicases
DNA-Binding Proteins
Human Herpesvirus 1
Viruses
Homologous Recombination
Molecules
Joints
Rec A Recombinases
DNA Viruses
Recombinant DNA
DNA
Genetic Recombination
Genes
Adenosine Triphosphate
Genome
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry

Cite this

In vitro strand exchange promoted by the herpes simplex virus type-1 single strand DNA-binding protein (ICP8) and DNA helicase-primase. / Nimonkar, Amitabh V.; Boehmer, Paul E.

In: Journal of Biological Chemistry, Vol. 277, No. 17, 26.04.2002, p. 15182-15189.

Research output: Contribution to journalArticle

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