Open AccessThe Virion Host Shutoff Protein (U L 41) of Herpes Simplex Virus 1 Is an Endoribonuclease with a Substrate Specificity Similar to That of RNase A
Author(s) -
Brunella Taddeo,
Bernard Roizman
Publication year - 2006
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01008-06
Subject(s) - endoribonuclease , biology , rna , microbiology and biotechnology , rnase p , oligonucleotide , nuclease , cytidine , ribonucleoprotein , uridine , herpes simplex virus , rnase h , biochemistry , enzyme , virus , virology , gene
Earlier, our laboratory reported that purified glutathioneS -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 tovhs .