Tristetraprolin Recruits the Herpes Simplex Virion Host Shutoff RNase to AU-Rich Elements in Stress Response mRNAs To Enable Their Cleavage

Journal of Virology
Minfeng ShuBernard Roizman

Abstract

Herpes simplex viruses (HSV) package and bring into cells an RNase designated virion host shutoff (VHS) RNase. In infected cells, the VHS RNase targets primarily stress response mRNAs characterized by the presence of AU-rich elements in their 3' untranslated regions (UTRs). In uninfected cells, these RNAs are sequestered in exosomes or P bodies by host proteins that bind to the AU-rich elements. In infected cells, the AU-rich RNAs are deadenylated and cleaved close to the AU-rich elements, leading to long-term persistence of nontranslatable RNAs consisting of the 5' portions of the cleavage products. The host proteins that bind to the AU-rich elements are either resident in cells (e.g., TIA-1) or induced (e.g., tristetraprolin). Earlier, this laboratory reported that tristetraprolin binds VHS RNase. To test the hypothesis that tristetraprolin directs VHS RNase to the AU-rich elements, we mapped the domains of VHS and tristetraprolin required for their interactions. We report that VHS binds to the domain of tristetraprolin that enables its interaction with RNA. A single amino acid substitution in that domain abolished the interaction with RNA but did not block the binding to VHS RNase. In transfected cells, the mutant but not th...Continue Reading

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Citations

Aug 26, 2015·Proceedings of the National Academy of Sciences of the United States of America·Minfeng ShuBernard Roizman
Sep 22, 2016·Critical Reviews in Biochemistry and Molecular Biology·Marni S CrowIleana M Cristea
May 12, 2018·Future Virology·Liang GuoPaul R Bohjanen
Dec 20, 2019·Therapeutic Advances in Respiratory Disease·Abdelnaby KhalyfaDavid Gozal
Nov 6, 2020·Journal of Virology·Caroline C FriedelLars Dölken

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