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PMID: 1650468 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The herpes simplex virus 1 segment inversion site is specifically cleaved by a virus-induced nuclear endonuclease.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 15 ·1991-08-01 ·Pages 6432-6

Wohlrab F, Chatterjee S, Wells RD

Abstract

Nuclear extracts from several tissue culture cell lines (human, primate, and murine) contain an endonuclease that specifically cleaves sequences at the herpes simplex virus 1 (HSV-1) segment inversion site. Mapping studies identified the preferential site of cleavage as a set of tandemly repeated dodecamers, the DR2 repeats. Endonuclease levels vary according to the proliferative state of the cell; little or no activity is detectable in extracts from quiescent cells, whereas high levels are expressed in dividing cells. Also, infection of density-arrested BSC-1 cells with HSV-1 induces a substantial increase (at least 35-fold) in endonucleolytic activity, which is first detectable at about 1 hr after infection at 32 degrees C. The elevated levels of enzyme activity then persist throughout the viral life cycle. In addition to the HSV-1 DR2 repeats, certain other G+C-rich sequences with an asymmetric distribution of purines and pyrimidines on the DNA strands and with appropriate sequences and lengths are substrates for the nuclease. These data indicate that target site recognition by the enzyme is conformation specific rather than sequence specific.

MeSH Terms
Animals Base Sequence Cell Line Cell Nucleus/enzymology Cell Transformation, Viral Chromosome Inversion DNA, Viral/genetics,metabolism Endonucleases/metabolism Kinetics Molecular Sequence Data Plasmids Repetitive Sequences, Nucleic Acid Simplexvirus/genetics,metabolism Substrate Specificity
Chemicals
DNA, Viral Endonucleases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wohlrab F
Department of Biochemistry, School of Medicine, University of Alabama, Birmingham 35294.
Chatterjee S
Wells R D
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43 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.15.6432
Published
1991-08-01
Pages
6432-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC52099
Subset
IM
Grants
NIAID NIH HHS · AI27767-02 · United States
External Links
PubMed source DOI: 10.1073/pnas.88.15.6432 PMC Full Text View journal details
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