A plant virus movement protein regulates the Gcn2p kinase in budding yeast.

Virus life cycle heavily depends on their ability to command the host machinery in order to translate their genomes. Animal viruses have been shown to interfere with host translation machinery by expressing viral proteins that either maintain or inhibit eIF2α function by phosphorylation. However, th...

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Autores principales:	Frederic Aparicio, Rafael Aparicio-Sanchis, José Gadea, Jesús Ángel Sánchez-Navarro, Vicente Pallás, José Ramón Murguía
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/45d3c49a6d474752b03bc02c9e052efa
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spelling	oai:doaj.org-article:45d3c49a6d474752b03bc02c9e052efa2021-11-18T07:34:43ZA plant virus movement protein regulates the Gcn2p kinase in budding yeast.1932-620310.1371/journal.pone.0027409https://doaj.org/article/45d3c49a6d474752b03bc02c9e052efa2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22087310/?tool=EBIhttps://doaj.org/toc/1932-6203Virus life cycle heavily depends on their ability to command the host machinery in order to translate their genomes. Animal viruses have been shown to interfere with host translation machinery by expressing viral proteins that either maintain or inhibit eIF2α function by phosphorylation. However, this interference mechanism has not been described for any plant virus yet. Prunnus necrotic ringspot virus (PNRSV) is a serious pathogen of cultivated stone fruit trees. The movement protein (MP) of PNRSV is necessary for the cell-to-cell movement of the virus. By using a yeast-based approach we have found that over-expression of the PNRSV MP caused a severe growth defect in yeast cells. cDNA microarrays analysis carried out to characterise at the molecular level the growth interference phenotype reported the induction of genes related to amino acid deprivation suggesting that expression of MP activates the GCN pathway in yeast cells. Accordingly, PNRSV MP triggered activation of the Gcn2p kinase, as judged by increased eIF2α phosphorylation. Activation of Gcn2p by MP expression required a functional Tor1p kinase, since rapamycin treatment alleviated the yeast cell growth defect and blocked eIF2α phosphorylation triggered by MP expression. Overall, these findings uncover a previously uncharacterised function for PNRSV MP viral protein, and point out at Tor1p and Gcn2p kinases as candidate susceptibility factors for plant viral infections.Frederic AparicioRafael Aparicio-SanchisJosé GadeaJesús Ángel Sánchez-NavarroVicente PallásJosé Ramón MurguíaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 11, p e27409 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Frederic Aparicio Rafael Aparicio-Sanchis José Gadea Jesús Ángel Sánchez-Navarro Vicente Pallás José Ramón Murguía A plant virus movement protein regulates the Gcn2p kinase in budding yeast.
description	Virus life cycle heavily depends on their ability to command the host machinery in order to translate their genomes. Animal viruses have been shown to interfere with host translation machinery by expressing viral proteins that either maintain or inhibit eIF2α function by phosphorylation. However, this interference mechanism has not been described for any plant virus yet. Prunnus necrotic ringspot virus (PNRSV) is a serious pathogen of cultivated stone fruit trees. The movement protein (MP) of PNRSV is necessary for the cell-to-cell movement of the virus. By using a yeast-based approach we have found that over-expression of the PNRSV MP caused a severe growth defect in yeast cells. cDNA microarrays analysis carried out to characterise at the molecular level the growth interference phenotype reported the induction of genes related to amino acid deprivation suggesting that expression of MP activates the GCN pathway in yeast cells. Accordingly, PNRSV MP triggered activation of the Gcn2p kinase, as judged by increased eIF2α phosphorylation. Activation of Gcn2p by MP expression required a functional Tor1p kinase, since rapamycin treatment alleviated the yeast cell growth defect and blocked eIF2α phosphorylation triggered by MP expression. Overall, these findings uncover a previously uncharacterised function for PNRSV MP viral protein, and point out at Tor1p and Gcn2p kinases as candidate susceptibility factors for plant viral infections.
format	article
author	Frederic Aparicio Rafael Aparicio-Sanchis José Gadea Jesús Ángel Sánchez-Navarro Vicente Pallás José Ramón Murguía
author_facet	Frederic Aparicio Rafael Aparicio-Sanchis José Gadea Jesús Ángel Sánchez-Navarro Vicente Pallás José Ramón Murguía
author_sort	Frederic Aparicio
title	A plant virus movement protein regulates the Gcn2p kinase in budding yeast.
title_short	A plant virus movement protein regulates the Gcn2p kinase in budding yeast.
title_full	A plant virus movement protein regulates the Gcn2p kinase in budding yeast.
title_fullStr	A plant virus movement protein regulates the Gcn2p kinase in budding yeast.
title_full_unstemmed	A plant virus movement protein regulates the Gcn2p kinase in budding yeast.
title_sort	plant virus movement protein regulates the gcn2p kinase in budding yeast.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/45d3c49a6d474752b03bc02c9e052efa
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A plant virus movement protein regulates the Gcn2p kinase in budding yeast.

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