Journal
JOURNAL OF VIROLOGY
Volume 80, Issue 18, Pages 9341-9345Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01008-06
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Funding
- NCI NIH HHS [CA 88860, R01 CA083939, CA 78766, R37 CA078766, R01 CA088860, CA 71933, P01 CA071933, P01 CA087661, CA 87661, R01 CA078766, CA 83939] Funding Source: Medline
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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.
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