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The herpes simplex virus type 1 helicase-primase. Analysis of helicase activity.

Journal article
Authors Maria Falkenberg
Per Elias
I R Lehman
Published in The Journal of biological chemistry
Volume 273
Issue 48
Pages 32154-7
ISSN 0021-9258
Publication year 1998
Published at Institute of Medical Biochemistry
Pages 32154-7
Language en
Keywords Base Sequence, DNA Helicases, metabolism, DNA Primase, DNA Replication, DNA-Binding Proteins, metabolism, DNA-Directed DNA Polymerase, metabolism, Herpesvirus 1, Human, enzymology, Magnesium, pharmacology, Molecular Sequence Data, Oligodeoxyribonucleotides, chemistry, metabolism, Substrate Specificity, Templates, Genetic, Viral Proteins, metabolism, Virus Replication
Subject categories Chemistry


The rate of unwinding of duplex DNA by the herpes simplex virus type 1 (HSV-1)-encoded helicase-primase (primosome) was determined by measuring the rate of appearance of single strands from a circular duplex DNA containing a 40-nucleotide 5' single-stranded tail, i.e. a preformed replication fork, in the presence of the HSV-1 single strand DNA-binding protein, infected cell protein 8 (ICP8). With this substrate, the rate at low ionic strength was highly sensitive to Mg2+ concentration. The Mg2+ dependence was a reflection of both the requirement for ICP8 for helicase activity and the ability of ICP8 to reverse the helicase reaction as a consequence of its capacity to anneal homologous single strands at Mg2+ concentrations in excess of 3 mM. The rate of unwinding of duplex DNA by the HSV-1 primosome was also determined indirectly by measuring the rate of leading strand synthesis with a preformed replication fork as template in the presence of the T7 DNA polymerase. The value of 60-65 base pairs unwound/s by both methods is consistent with the rate of 50 base pairs/s estimated for the rate of fork movement in vivo during replication of pseudorabies virus, another herpesvirus. Interaction with the helicase-primase did not increase its helicase activity.

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