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An N-Terminal Fragment of Yeast Ribosomal Protein L3 Inhibits the Cytotoxicity of Pokeweed Antiviral Protein in Saccharomyces cerevisiae
We have previously shown that ribosomal protein L3 is required for pokeweed antiviral protein (PAP), a type I ribosome inactivating protein, to bind to ribosomes and depurinate the α-sarcin/ricin loop (SRL) in yeast. Co-expression of the N-terminal 99 amino acids of yeast L3 (L3Δ99) with PAP in tran...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4014737/ https://www.ncbi.nlm.nih.gov/pubmed/24732204 http://dx.doi.org/10.3390/toxins6041349 |
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author | Di, Rong Tumer, Nilgun E. |
author_facet | Di, Rong Tumer, Nilgun E. |
author_sort | Di, Rong |
collection | PubMed |
description | We have previously shown that ribosomal protein L3 is required for pokeweed antiviral protein (PAP), a type I ribosome inactivating protein, to bind to ribosomes and depurinate the α-sarcin/ricin loop (SRL) in yeast. Co-expression of the N-terminal 99 amino acids of yeast L3 (L3Δ99) with PAP in transgenic tobacco plants completely abolished the toxicity of PAP. In this study, we investigated the interaction between PAP and L3Δ99 in Saccharomyces cerevisiae. Yeast cells co-transformed with PAP and L3Δ99 showed markedly reduced growth inhibition and reduced rRNA depurination by PAP, compared to cells transformed with PAP alone. Co-transformation of yeast with PAP and L3Δ21 corresponding to the highly conserved N-terminal 21 amino acids of L3Δ99, reduced the cytotoxicity of PAP. PAP mRNA and protein levels were elevated and L3Δ99 or L3Δ21 mRNA and protein levels were reduced in yeast co-transformed with PAP and L3Δ99 or with PAP and L3Δ21, respectively. PAP interacted with L3Δ21 in yeast cells in vivo and by Biacore analysis in vitro, suggesting that the interaction between L3Δ21 and PAP may inhibit PAP-mediated depurination of the SRL, leading to a reduction in the cytotoxicity of PAP. |
format | Online Article Text |
id | pubmed-4014737 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-40147372014-05-09 An N-Terminal Fragment of Yeast Ribosomal Protein L3 Inhibits the Cytotoxicity of Pokeweed Antiviral Protein in Saccharomyces cerevisiae Di, Rong Tumer, Nilgun E. Toxins (Basel) Article We have previously shown that ribosomal protein L3 is required for pokeweed antiviral protein (PAP), a type I ribosome inactivating protein, to bind to ribosomes and depurinate the α-sarcin/ricin loop (SRL) in yeast. Co-expression of the N-terminal 99 amino acids of yeast L3 (L3Δ99) with PAP in transgenic tobacco plants completely abolished the toxicity of PAP. In this study, we investigated the interaction between PAP and L3Δ99 in Saccharomyces cerevisiae. Yeast cells co-transformed with PAP and L3Δ99 showed markedly reduced growth inhibition and reduced rRNA depurination by PAP, compared to cells transformed with PAP alone. Co-transformation of yeast with PAP and L3Δ21 corresponding to the highly conserved N-terminal 21 amino acids of L3Δ99, reduced the cytotoxicity of PAP. PAP mRNA and protein levels were elevated and L3Δ99 or L3Δ21 mRNA and protein levels were reduced in yeast co-transformed with PAP and L3Δ99 or with PAP and L3Δ21, respectively. PAP interacted with L3Δ21 in yeast cells in vivo and by Biacore analysis in vitro, suggesting that the interaction between L3Δ21 and PAP may inhibit PAP-mediated depurination of the SRL, leading to a reduction in the cytotoxicity of PAP. MDPI 2014-04-11 /pmc/articles/PMC4014737/ /pubmed/24732204 http://dx.doi.org/10.3390/toxins6041349 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Di, Rong Tumer, Nilgun E. An N-Terminal Fragment of Yeast Ribosomal Protein L3 Inhibits the Cytotoxicity of Pokeweed Antiviral Protein in Saccharomyces cerevisiae |
title | An N-Terminal Fragment of Yeast Ribosomal Protein L3 Inhibits the Cytotoxicity of Pokeweed Antiviral Protein in Saccharomyces cerevisiae |
title_full | An N-Terminal Fragment of Yeast Ribosomal Protein L3 Inhibits the Cytotoxicity of Pokeweed Antiviral Protein in Saccharomyces cerevisiae |
title_fullStr | An N-Terminal Fragment of Yeast Ribosomal Protein L3 Inhibits the Cytotoxicity of Pokeweed Antiviral Protein in Saccharomyces cerevisiae |
title_full_unstemmed | An N-Terminal Fragment of Yeast Ribosomal Protein L3 Inhibits the Cytotoxicity of Pokeweed Antiviral Protein in Saccharomyces cerevisiae |
title_short | An N-Terminal Fragment of Yeast Ribosomal Protein L3 Inhibits the Cytotoxicity of Pokeweed Antiviral Protein in Saccharomyces cerevisiae |
title_sort | n-terminal fragment of yeast ribosomal protein l3 inhibits the cytotoxicity of pokeweed antiviral protein in saccharomyces cerevisiae |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4014737/ https://www.ncbi.nlm.nih.gov/pubmed/24732204 http://dx.doi.org/10.3390/toxins6041349 |
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