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The herpes simplex virus helicase-primase complex, a
heterotrimer of the UL5, UL8, and UL52 proteins, displays a single
predominant site of primer synthesis on
Volume 270,
Number 16,
Issue of April 21, pp. 9129-9136, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
X174 virion DNA (Tenney,
D. J., Hurlburt, W. W., Micheletti, P. M., Bifano, M., and Hamatake, R.
K. (1994) J. Biol. Chem. 269, 5030-5035). This site was
mapped and found to be deoxycytosine-rich, directing the synthesis of a
primer initiating with several guanine residues. The size and sequence
requirements for primer synthesis were determined using
oligonucleotides containing variations of the predominant template.
Although the efficiency of primer synthesis on oligonucleotides was
influenced by template size, it was absolutely dependent on nucleotide
sequence. Conversely, the ATPase activity on oligonucleotide templates
was dependent on template size rather than nucleotide sequence.
Furthermore, only oligonucleotides containing primase templates were
inhibitory in a coupled primase-polymerase assay using
X174 DNA
as template, suggesting that primer synthesis or primase turnover is
rate-limiting. Additionally, stimulation of helicase-primase by the UL8
component and that by the ICP8 protein were shown to differ
mechanistically using different templates: the UL8 component stimulated
the rate of primer synthesis on
X174 virion DNA and
oligonucleotide templates, while ICP8 stimulation occurred only on
X174 virion DNA.
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