Proteomic Analysis of Plasmodesmata From Populus Cell Suspension Cultures in Relation With Callose Biosynthesis.
Identifieur interne : 000D16 ( Main/Exploration ); précédent : 000D15; suivant : 000D17Proteomic Analysis of Plasmodesmata From Populus Cell Suspension Cultures in Relation With Callose Biosynthesis.
Auteurs : Felicia Leijon [Suède] ; Michael Melzer [Allemagne] ; Qi Zhou [Suède] ; Vaibhav Srivastava [Suède] ; Vincent Bulone [Suède, Australie]Source :
- Frontiers in plant science [ 1664-462X ] ; 2018.
Abstract
Plasmodesmata are channels that link adjacent cells in plant tissues through which molecular exchanges take place. They are involved in multiple processes vital to plant cells, such as responses to hormonal signaling or environmental challenges including osmotic stress, wounding and pathogen attack. Despite the importance of plasmodesmata, their proteome is not well-defined. Here, we have isolated fractions enriched in plasmodesmata from cell suspension cultures of Populus trichocarpa and identified 201 proteins that are enriched in these fractions, thereby providing further insight on the multiple functions of plasmodesmata. Proteomics analysis revealed an enrichment of proteins specifically involved in responses to stress, transport, metabolism and signal transduction. Consistent with the role of callose deposition and turnover in the closure and aperture of the plasmodesmata and our proteomic analysis, we demonstrate the enrichment of callose synthase activity in the plasmodesmata represented by several gene products. A new form of calcium-independent callose synthase activity was detected, in addition to the typical calcium-dependent enzyme activity, suggesting a role of calcium in the regulation of plasmodesmata through two forms of callose synthase activities. Our report provides the first proteomic investigation of the plasmodesmata from a tree species and the direct biochemical evidence for the occurrence of several forms of active callose synthases in these structures. Data are available via ProteomeXchange with identifier PXD010692.
DOI: 10.3389/fpls.2018.01681
PubMed: 30510561
PubMed Central: PMC6252348
Affiliations:
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Cultures in Relation With Callose Biosynthesis.</title><author><name sortKey="Leijon, Felicia" sort="Leijon, Felicia" uniqKey="Leijon F" first="Felicia" last="Leijon">Felicia Leijon</name><affiliation wicri:level="3"><nlm:affiliation>Division of Glycoscience, School of Engineering Sciences in Chemistry, Biotechnology and Health, Royal Institute of Technology, AlbaNova University Centre, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Division of Glycoscience, School of Engineering Sciences in Chemistry, Biotechnology and Health, Royal Institute of Technology, AlbaNova University Centre, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Melzer, Michael" sort="Melzer, Michael" uniqKey="Melzer M" first="Michael" last="Melzer">Michael Melzer</name><affiliation wicri:level="1"><nlm:affiliation>Leibniz Institute of Plant Genetics and Crop Plant Research, Gatersleben, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Leibniz Institute of Plant Genetics and Crop Plant Research, Gatersleben</wicri:regionArea><wicri:noRegion>Gatersleben</wicri:noRegion><wicri:noRegion>Gatersleben</wicri:noRegion><wicri:noRegion>Gatersleben</wicri:noRegion></affiliation></author><author><name sortKey="Zhou, Qi" sort="Zhou, Qi" uniqKey="Zhou Q" first="Qi" last="Zhou">Qi Zhou</name><affiliation wicri:level="3"><nlm:affiliation>Division of Glycoscience, School of Engineering Sciences in Chemistry, Biotechnology and Health, Royal Institute of Technology, AlbaNova University Centre, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Division of Glycoscience, School of Engineering Sciences in Chemistry, Biotechnology and Health, Royal Institute of Technology, AlbaNova University Centre, Stockholm</wicri:regionArea><placeName><settlement 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Bulone</name><affiliation wicri:level="3"><nlm:affiliation>Division of Glycoscience, School of Engineering Sciences in Chemistry, Biotechnology and Health, Royal Institute of Technology, AlbaNova University Centre, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Division of Glycoscience, School of Engineering Sciences in Chemistry, Biotechnology and Health, Royal Institute of Technology, AlbaNova University Centre, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation><affiliation wicri:level="1"><nlm:affiliation>ARC Centre of Excellence in Plant Cell Walls and School of Agriculture, Food and Wine, The University of Adelaide, Adelaide, SA, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>ARC Centre of Excellence in Plant Cell Walls and School of Agriculture, Food and Wine, The University of Adelaide, Adelaide, SA</wicri:regionArea><wicri:noRegion>SA</wicri:noRegion></affiliation></author></analytic><series><title level="j">Frontiers in plant science</title><idno type="ISSN">1664-462X</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plasmodesmata are channels that link adjacent cells in plant tissues through which molecular exchanges take place. They are involved in multiple processes vital to plant cells, such as responses to hormonal signaling or environmental challenges including osmotic stress, wounding and pathogen attack. Despite the importance of plasmodesmata, their proteome is not well-defined. Here, we have isolated fractions enriched in plasmodesmata from cell suspension cultures of <i>Populus trichocarpa</i> and identified 201 proteins that are enriched in these fractions, thereby providing further insight on the multiple functions of plasmodesmata. Proteomics analysis revealed an enrichment of proteins specifically involved in responses to stress, transport, metabolism and signal transduction. Consistent with the role of callose deposition and turnover in the closure and aperture of the plasmodesmata and our proteomic analysis, we demonstrate the enrichment of callose synthase activity in the plasmodesmata represented by several gene products. A new form of calcium-independent callose synthase activity was detected, in addition to the typical calcium-dependent enzyme activity, suggesting a role of calcium in the regulation of plasmodesmata through two forms of callose synthase activities. Our report provides the first proteomic investigation of the plasmodesmata from a tree species and the direct biochemical evidence for the occurrence of several forms of active callose synthases in these structures. Data are available via ProteomeXchange with identifier PXD010692.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">30510561</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-462X</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>Frontiers in plant science</Title><ISOAbbreviation>Front Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Proteomic Analysis of Plasmodesmata From <i>Populus</i> Cell Suspension Cultures in Relation With Callose Biosynthesis.</ArticleTitle><Pagination><MedlinePgn>1681</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fpls.2018.01681</ELocationID><Abstract><AbstractText>Plasmodesmata are channels that link adjacent cells in plant tissues through which molecular exchanges take place. They are involved in multiple processes vital to plant cells, such as responses to hormonal signaling or environmental challenges including osmotic stress, wounding and pathogen attack. Despite the importance of plasmodesmata, their proteome is not well-defined. Here, we have isolated fractions enriched in plasmodesmata from cell suspension cultures of <i>Populus trichocarpa</i> and identified 201 proteins that are enriched in these fractions, thereby providing further insight on the multiple functions of plasmodesmata. Proteomics analysis revealed an enrichment of proteins specifically involved in responses to stress, transport, metabolism and signal transduction. Consistent with the role of callose deposition and turnover in the closure and aperture of the plasmodesmata and our proteomic analysis, we demonstrate the enrichment of callose synthase activity in the plasmodesmata represented by several gene products. A new form of calcium-independent callose synthase activity was detected, in addition to the typical calcium-dependent enzyme activity, suggesting a role of calcium in the regulation of plasmodesmata through two forms of callose synthase activities. Our report provides the first proteomic investigation of the plasmodesmata from a tree species and the direct biochemical evidence for the occurrence of several forms of active callose synthases in these structures. 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last="Srivastava">Vaibhav Srivastava</name><name sortKey="Zhou, Qi" sort="Zhou, Qi" uniqKey="Zhou Q" first="Qi" last="Zhou">Qi Zhou</name></country><country name="Allemagne"><noRegion><name sortKey="Melzer, Michael" sort="Melzer, Michael" uniqKey="Melzer M" first="Michael" last="Melzer">Michael Melzer</name></noRegion></country><country name="Australie"><noRegion><name sortKey="Bulone, Vincent" sort="Bulone, Vincent" uniqKey="Bulone V" first="Vincent" last="Bulone">Vincent Bulone</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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