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Open AccessArticle

Characteristics of Human OAS1 Isoform Proteins

by 1,†, 1,2,† and 1,*
1
Department of Biology, Georgia State University, Atlanta, GA 30303, USA
2
Research Center for Emerging Infections and Zoonosis (RIZ), University of Veterinary Medicine Hannover, 30559 Hannover, Germany
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Viruses 2020, 12(2), 152; https://doi.org/10.3390/v12020152
Received: 1 November 2019 / Revised: 20 January 2020 / Accepted: 22 January 2020 / Published: 29 January 2020
(This article belongs to the Special Issue Viruses and the OAS-RNase L Pathway)
The human OAS1 (hOAS1) gene produces multiple possible isoforms due to alternative splicing events and sequence variation among individuals, some of which affect splicing. The unique C-terminal sequences of the hOAS1 isoforms could differentially affect synthetase activity, protein stability, protein partner interactions and/or cellular localization. Recombinant p41, p42, p44, p46, p48, p49 and p52 hOAS1 isoform proteins expressed in bacteria were each able to synthesize trimer and higher order 2′-5′ linked oligoadenylates in vitro in response to poly(I:C). The p42, p44, p46, p48 and p52 isoform proteins were each able to induce RNase-mediated rRNA cleavage in response to poly(I:C) when overexpressed in HEK293 cells. The expressed levels of the p42 and p46 isoform proteins were higher than those of the other isoforms, suggesting increased stability in mammalian cells. In a yeast two-hybrid screen, Fibrillin1 (FBN1) was identified as a binding partner for hOAS1 p42 isoform, and Supervillin (SVIL) as a binding partner for the p44 isoform. The p44-SVIL interaction was supported by co-immunoprecipitation data from mammalian cells. The data suggest that the unique C-terminal regions of hOAS1 isoforms may mediate the recruitment of different partners, alternative functional capacities and/or different cellular localization. View Full-Text
Keywords: human OAS1 isoforms; 2-5A; rRNA cleavage; Fibrillin1; supervillin human OAS1 isoforms; 2-5A; rRNA cleavage; Fibrillin1; supervillin
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MDPI and ACS Style

Di, H.; Elbahesh, H.; Brinton, M.A. Characteristics of Human OAS1 Isoform Proteins. Viruses 2020, 12, 152. https://doi.org/10.3390/v12020152

AMA Style

Di H, Elbahesh H, Brinton MA. Characteristics of Human OAS1 Isoform Proteins. Viruses. 2020; 12(2):152. https://doi.org/10.3390/v12020152

Chicago/Turabian Style

Di, Han; Elbahesh, Husni; Brinton, Margo A. 2020. "Characteristics of Human OAS1 Isoform Proteins" Viruses 12, no. 2: 152. https://doi.org/10.3390/v12020152

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