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PMID: 2840645 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

A DNA helicase induced by herpes simplex virus type 1.

Nucleic acids research ·Vol. 16 ·No. 14A ·1988-07-25 ·Pages 6585-96

Crute JJ, Mocarski ES, Lehman IR

Abstract

We have identified and partially purified a DNA-dependent ATPase that is present specifically in herpes simplex virus type 1-infected Vero cells. The enzyme which has a molecular weight of approximately 440,000 differs from the comparable host enzyme in its elution from phosphocellulose columns and in its nucleoside triphosphate specificity. The partially purified DNA-dependent ATPase is also a DNA helicase that couples ATP or GTP hydrolysis to the displacement of an oligonucleotide annealed to M13 single-stranded DNA. The enzyme requires a 3' single-stranded tail on the duplex substrate, suggesting that the polarity of unwinding is 5'----3' relative to the M13 DNA. The herpes specific DNA helicase may therefore translocate on the lagging strand in the semidiscontinuous replication of the herpes virus 1 genome.

MeSH Terms
Adenosine Triphosphatases/biosynthesis,isolation & purification Animals DNA Helicases/biosynthesis,isolation & purification Enzyme Induction Kinetics Simplexvirus/physiology Substrate Specificity Vero Cells
Chemicals
Adenosine Triphosphatases DNA Helicases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Crute J J
Department of Biochemistry, Stanford University School of Medicine, CA 94305.
Mocarski E S
Lehman I R
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20 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/16.14.6585
Published
1988-07-25
Pages
6585-96
Language
English
Region
England
NLM ID
0411011
PMCID
PMC338315
Subset
IM
Grants
NIAID NIH HHS · AI-20211 · United States
NCI NIH HHS · CA-09302 · United States
NIGMS NIH HHS · GM-06196 · United States
External Links
PubMed source DOI: 10.1093/nar/16.14.6585 PMC Full Text View journal details
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