A plant virus movement protein regulates the Gcn2p kinase in budding yeast.
Identifieur interne : 001358 ( Main/Exploration ); précédent : 001357; suivant : 001359A plant virus movement protein regulates the Gcn2p kinase in budding yeast.
Auteurs : Frederic Aparicio [Espagne] ; Rafael Aparicio-Sanchis ; José Gadea ; Jesús Ngel Sánchez-Navarro ; Vicente Pallás ; José Ram N MurguíaSource :
- PloS one [ 1932-6203 ] ; 2011.
Descripteurs français
- KwdFr :
- Activation de la transcription (MeSH), Maladies virales (étiologie), Protein-Serine-Threonine Kinases (génétique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de mouvement des virus de plantes (physiologie), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (virologie).
- MESH :
- enzymologie : Saccharomyces cerevisiae.
- génétique : Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae.
- physiologie : Protéines de mouvement des virus de plantes.
- virologie : Saccharomyces cerevisiae.
- étiologie : Maladies virales.
- Activation de la transcription.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- chemical , physiology : Plant Viral Movement Proteins.
- enzymology : Saccharomyces cerevisiae.
- etiology : Virus Diseases.
- virology : Saccharomyces cerevisiae.
- Transcriptional Activation.
Abstract
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.
DOI: 10.1371/journal.pone.0027409
PubMed: 22087310
PubMed Central: PMC3210792
Affiliations:
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uniqKey="Aparicio Sanchis R" first="Rafael" last="Aparicio-Sanchis">Rafael Aparicio-Sanchis</name></author><author><name sortKey="Gadea, Jose" sort="Gadea, Jose" uniqKey="Gadea J" first="José" last="Gadea">José Gadea</name></author><author><name sortKey="Sanchez Navarro, Jesus Ngel" sort="Sanchez Navarro, Jesus Ngel" uniqKey="Sanchez Navarro J" first="Jesús Ngel" last="Sánchez-Navarro">Jesús Ngel Sánchez-Navarro</name></author><author><name sortKey="Pallas, Vicente" sort="Pallas, Vicente" uniqKey="Pallas V" first="Vicente" last="Pallás">Vicente Pallás</name></author><author><name sortKey="Murguia, Jose Ram N" sort="Murguia, Jose Ram N" uniqKey="Murguia J" first="José Ram N" last="Murguía">José Ram N Murguía</name></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Plant Viral Movement Proteins (physiology)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Saccharomyces cerevisiae (enzymology)</term><term>Saccharomyces cerevisiae (virology)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Transcriptional Activation (MeSH)</term><term>Virus Diseases (etiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation de la transcription (MeSH)</term><term>Maladies virales (étiologie)</term><term>Protein-Serine-Threonine Kinases (génétique)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de mouvement des virus de plantes (physiologie)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Saccharomyces cerevisiae (virologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Protein-Serine-Threonine Kinases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Plant Viral Movement Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="etiology" xml:lang="en"><term>Virus Diseases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines de mouvement des virus de plantes</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="étiologie" xml:lang="fr"><term>Maladies virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Transcriptional Activation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation de la transcription</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22087310</PMID><DateCompleted><Year>2012</Year><Month>05</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><Issue>11</Issue><PubDate><Year>2011</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>A plant virus movement protein regulates the Gcn2p kinase in budding yeast.</ArticleTitle><Pagination><MedlinePgn>e27409</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0027409</ELocationID><Abstract><AbstractText>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. 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sortKey="Gadea, Jose" sort="Gadea, Jose" uniqKey="Gadea J" first="José" last="Gadea">José Gadea</name><name sortKey="Murguia, Jose Ram N" sort="Murguia, Jose Ram N" uniqKey="Murguia J" first="José Ram N" last="Murguía">José Ram N Murguía</name><name sortKey="Pallas, Vicente" sort="Pallas, Vicente" uniqKey="Pallas V" first="Vicente" last="Pallás">Vicente Pallás</name><name sortKey="Sanchez Navarro, Jesus Ngel" sort="Sanchez Navarro, Jesus Ngel" uniqKey="Sanchez Navarro J" first="Jesús Ngel" last="Sánchez-Navarro">Jesús Ngel Sánchez-Navarro</name></noCountry><country name="Espagne"><noRegion><name sortKey="Aparicio, Frederic" sort="Aparicio, Frederic" uniqKey="Aparicio F" first="Frederic" last="Aparicio">Frederic Aparicio</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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