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J. Biol. Chem., Vol. 275, Issue 47, 36506-36508, November 24, 2000

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 275/47/36506    most recent C000585200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sekino, Y. Articles by Verdine, G. L. Search for Related Content PubMed PubMed Citation Articles by Sekino, Y. Articles by Verdine, G. L. Social Bookmarking                      What's this?

ACCELERATED PUBLICATION
Selective Inhibition of Herpes Simplex Virus Type-1 Uracil-DNA Glycosylase by Designed Substrate Analogs^*,

Yukiko Sekino, Steven D. Bruner, and Gregory L. Verdine

From the Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138

Cytosine deamination and the misincorporation of 2'-dUrd into DNA during replication result in the presence of uracil in DNA. Uracil-DNA glycosylases (UDGs) initiate the excision repair of this aberrant base by catalyzing the hydrolysis of the N-glycosidic bond. UDGs are expressed by nearly all known organisms, including some viruses, in which the functional role of the UDG protein remains unresolved. This issue could in principle be addressed by the availability of designed synthetic inhibitors that target the viral UDG without affecting the endogenous human UDG. Here, we report that double-stranded and single-stranded oligonucleotides incorporating either of two dUrd analogs tightly bind and inhibit the activity of herpes simplex virus type-1 (HSV-1) UDG. Both inhibitors are exquisitely specific for the HSV-1 UDG over the human UDG. These inhibitors should prove useful in structural studies aimed at understanding substrate recognition and catalysis by UDGs, as well as in elucidating the biologic role of UDGs in the life cycle of herpesviruses.

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