The virion host shutoff protein (UL41) of herpes simplex virus 11 is an endoribonuclease with a substrate specificity similar to that of RNase A

Brunella Taddeo, Bernard Roizman

Research output: Contribution to journalArticlepeer-review

80 Scopus citations

Abstract

Earlier, our laboratory reported that purified glutathione S-transferase-virion host shutoff (GST-vhs) protein exhibited endoribonucleolytic activity in in vitro assays using as substrates in vitro-transcribed regions of IEX-1 mRNA. Here, we report that studies of the cleavage patterns of synthetic RNA oligonucleotides defined the activity of GST-vhs as being similar to that of RNase A. Thus, GST-vhs cleaved the RNA at the 3′ end of single-stranded cytidine and uridine residues. Since the GST-mvhs nuclease-defective mutant protein failed to cleave the synthetic RNAs, the results unambiguously attribute the activity to vhs.

Original languageEnglish
Pages (from-to)9341-9345
Number of pages5
JournalJournal of Virology
Volume80
Issue number18
DOIs
StatePublished - Sep 2006

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