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(Received for publication, October 7, 1996, and in revised form, November 29, 1996)
From the Herpes simplex virus type 1 encodes a
heterotrimeric helicase-primase composed of the products of the UL5,
UL52, and UL8 genes. UL5 possesses six motifs conserved among
superfamily 1 of helicase proteins. Substitutions of conserved residues
in each motif abolishes DNA replication in vivo (Zhu, L.,
and Weller, S. K. (1992) J. Virol. 66, 469-479).
Purified UL5·52 harboring a Gly to Ala change in motif V retains
primase and helicase activities in vitro but exhibits a
higher KM for single-stranded DNA and lower DNA-dependent ATPase activity (Graves-Woodward, K. L., and
Weller, S. K. (1996) J. Biol. Chem. 272, 13629-13635). We have purified and characterized six other
subcomplexes with residue changes in the UL5 helicase motifs. Each
variant subcomplex displays at least wild type or greater levels of
primase and DNA binding activities, but all are defective in helicase
activity. Mutations in motifs I and II exhibit profound decreases in
DNA-dependent ATPase activity. Mutations in motifs III-VI
decrease DNA-dependent ATPase activity 3-6-fold. Since
mutations in motifs III, IV, V, and VI do not eliminate ATP hydrolysis
or DNA binding, we propose that they may be involved in the coupling of
these two activities to the process of DNA unwinding. This analysis
represents the first comprehensive structure-function analysis of the
conserved motifs in helicase superfamily 1.
Volume 272, Number 7,
Issue of February 14, 1997
pp. 4623-4630
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Department of Microbiology, The University
of Connecticut Health Center, Farmington, Connecticut 06030-3205 and
the ¶ Laboratory of Viral Diseases, NIAID, National Institutes of
Health, Bethesda, Maryland 20892
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