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J Biol Chem, Vol. 273, Issue 48, 32154-32157, November 27, 1998
From the 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.
The Herpes Simplex Virus Type 1 Helicase-primase
ANALYSIS OF HELICASE ACTIVITY
§,
Department of Biochemistry, Beckman Center,
Stanford University, Stanford, California 94305-5307 and
§ Department of Medical Biochemistry, Goteborg University,
S-413 90 Goteborg, Sweden
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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