Non-dispersive phloem-protein bodies (NPBs) of Populus trichocarpa consist of a SEOR protein and do not respond to cell wounding and Ca2.
Identifieur interne : 000D67 ( Main/Exploration ); précédent : 000D66; suivant : 000D68Non-dispersive phloem-protein bodies (NPBs) of Populus trichocarpa consist of a SEOR protein and do not respond to cell wounding and Ca2.
Auteurs : Daniel L. Mullendore [États-Unis] ; Timothy Ross-Elliott [États-Unis] ; Yan Liu [États-Unis] ; Hanjo H. Hellmann [États-Unis] ; Eric H. Roalson [États-Unis] ; Winfried S. Peters [États-Unis] ; Michael Knoblauch [États-Unis]Source :
- PeerJ [ 2167-8359 ] ; 2018.
Abstract
Differentiating sieve elements in the phloem of angiosperms produce abundant phloem-specific proteins before their protein synthesis machinery is degraded. These P-proteins initially form dense bodies, which disperse into individual filaments when the sieve element matures. In some cases, however, the dense protein agglomerations remain intact and are visible in functional sieve tubes as non-dispersive P-protein bodies, or NPBs. Species exhibiting NPBs are distributed across the entire angiosperm clade. We found that NPBs in the model tree, Populus trichocarpa, resemble the protein bodies described from other species of the order Malpighiales as they all consist of coaligned tubular fibrils bundled in hexagonal symmetry. NPBs of all Malpighiales tested proved unresponsive to sieve tube wounding and Ca2+. The P. trichocarpa NPBs consisted of a protein encoded by a gene that in the genome database of this species had been annotated as a homolog of SEOR1 (sieve element occlusion-related 1) in Arabidopsis. Sequencing of the gene in our plants corroborated this interpretation, and we named the gene PtSEOR1. Previously characterized SEOR proteins form irregular masses of P-protein slime in functional sieve tubes. We conclude that a subgroup of these proteins is involved in the formation of NPBs at least in the Malpighiales, and that these protein bodies have no role in rapid wound responses of the sieve tube network.
DOI: 10.7717/peerj.4665
PubMed: 29682428
PubMed Central: PMC5909683
Affiliations:
- États-Unis
- Caroline du Nord, Washington (État)
- Chapel Hill (Caroline du Nord)
- Université de Caroline du Nord à Chapel Hill
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Mullendore</name><affiliation wicri:level="2"><nlm:affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Biological Sciences, Washington State University, Pullman, WA</wicri:regionArea><placeName><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Ross Elliott, Timothy" sort="Ross Elliott, Timothy" uniqKey="Ross Elliott T" first="Timothy" last="Ross-Elliott">Timothy Ross-Elliott</name><affiliation wicri:level="4"><nlm:affiliation>Biology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC</wicri:regionArea><placeName><region type="state">Caroline du Nord</region><settlement type="city">Chapel Hill (Caroline du Nord)</settlement></placeName><orgName type="university">Université de Caroline du Nord à Chapel Hill</orgName></affiliation></author><author><name sortKey="Liu, Yan" sort="Liu, Yan" uniqKey="Liu Y" first="Yan" last="Liu">Yan Liu</name><affiliation wicri:level="2"><nlm:affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Biological Sciences, Washington State University, Pullman, WA</wicri:regionArea><placeName><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Hellmann, Hanjo H" sort="Hellmann, Hanjo H" uniqKey="Hellmann H" first="Hanjo H" last="Hellmann">Hanjo H. Hellmann</name><affiliation wicri:level="2"><nlm:affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Biological Sciences, Washington State University, Pullman, WA</wicri:regionArea><placeName><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Roalson, Eric H" sort="Roalson, Eric H" uniqKey="Roalson E" first="Eric H" last="Roalson">Eric H. 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Peters</name><affiliation wicri:level="2"><nlm:affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Biological Sciences, Washington State University, Pullman, WA</wicri:regionArea><placeName><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Knoblauch, Michael" sort="Knoblauch, Michael" uniqKey="Knoblauch M" first="Michael" last="Knoblauch">Michael Knoblauch</name><affiliation wicri:level="2"><nlm:affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Biological Sciences, Washington State University, Pullman, WA</wicri:regionArea><placeName><region type="state">Washington (État)</region></placeName></affiliation></author></analytic><series><title level="j">PeerJ</title><idno type="ISSN">2167-8359</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">Differentiating sieve elements in the phloem of angiosperms produce abundant phloem-specific proteins before their protein synthesis machinery is degraded. These P-proteins initially form dense bodies, which disperse into individual filaments when the sieve element matures. In some cases, however, the dense protein agglomerations remain intact and are visible in functional sieve tubes as non-dispersive P-protein bodies, or NPBs. Species exhibiting NPBs are distributed across the entire angiosperm clade. We found that NPBs in the model tree, <i>Populus trichocarpa</i>, resemble the protein bodies described from other species of the order Malpighiales as they all consist of coaligned tubular fibrils bundled in hexagonal symmetry. NPBs of all Malpighiales tested proved unresponsive to sieve tube wounding and Ca<sup>2+</sup>. The <i>P. trichocarpa</i> NPBs consisted of a protein encoded by a gene that in the genome database of this species had been annotated as a homolog of <i>SEOR1</i> (sieve element occlusion-related 1) in <i>Arabidopsis</i>. Sequencing of the gene in our plants corroborated this interpretation, and we named the gene <i>PtSEOR1</i>. Previously characterized SEOR proteins form irregular masses of P-protein slime in functional sieve tubes. We conclude that a subgroup of these proteins is involved in the formation of NPBs at least in the Malpighiales, and that these protein bodies have no role in rapid wound responses of the sieve tube network.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">29682428</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">2167-8359</ISSN><JournalIssue CitedMedium="Print"><Volume>6</Volume><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>PeerJ</Title><ISOAbbreviation>PeerJ</ISOAbbreviation></Journal><ArticleTitle>Non-dispersive phloem-protein bodies (NPBs) of <i>Populus trichocarpa</i> consist of a SEOR protein and do not respond to cell wounding and Ca<sup>2</sup>.</ArticleTitle><Pagination><MedlinePgn>e4665</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.7717/peerj.4665</ELocationID><Abstract><AbstractText>Differentiating sieve elements in the phloem of angiosperms produce abundant phloem-specific proteins before their protein synthesis machinery is degraded. These P-proteins initially form dense bodies, which disperse into individual filaments when the sieve element matures. In some cases, however, the dense protein agglomerations remain intact and are visible in functional sieve tubes as non-dispersive P-protein bodies, or NPBs. Species exhibiting NPBs are distributed across the entire angiosperm clade. We found that NPBs in the model tree, <i>Populus trichocarpa</i>, resemble the protein bodies described from other species of the order Malpighiales as they all consist of coaligned tubular fibrils bundled in hexagonal symmetry. NPBs of all Malpighiales tested proved unresponsive to sieve tube wounding and Ca<sup>2+</sup>. The <i>P. trichocarpa</i> NPBs consisted of a protein encoded by a gene that in the genome database of this species had been annotated as a homolog of <i>SEOR1</i> (sieve element occlusion-related 1) in <i>Arabidopsis</i>. Sequencing of the gene in our plants corroborated this interpretation, and we named the gene <i>PtSEOR1</i>. Previously characterized SEOR proteins form irregular masses of P-protein slime in functional sieve tubes. We conclude that a subgroup of these proteins is involved in the formation of NPBs at least in the Malpighiales, and that these protein bodies have no role in rapid wound responses of the sieve tube network.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mullendore</LastName><ForeName>Daniel L</ForeName><Initials>DL</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ross-Elliott</LastName><ForeName>Timothy</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Biology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Yan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hellmann</LastName><ForeName>Hanjo H</ForeName><Initials>HH</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roalson</LastName><ForeName>Eric H</ForeName><Initials>EH</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peters</LastName><ForeName>Winfried S</ForeName><Initials>WS</Initials><Identifier Source="ORCID">0000-0002-5061-1497</Identifier><AffiliationInfo><Affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Knoblauch</LastName><ForeName>Michael</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Washington State University, Pullman, WA, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>04</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PeerJ</MedlineTA><NlmUniqueID>101603425</NlmUniqueID><ISSNLinking>2167-8359</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Non-dispersive P-protein body</Keyword><Keyword MajorTopicYN="N">P-protein</Keyword><Keyword MajorTopicYN="N">Phloem transport</Keyword><Keyword MajorTopicYN="N">Populus trichocarpa</Keyword><Keyword MajorTopicYN="N">SEOR protein</Keyword><Keyword MajorTopicYN="N">Sieve element</Keyword></KeywordList><CoiStatement>The authors declare that they have no competing interests.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>02</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>04</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>4</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>4</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>4</Month><Day>24</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29682428</ArticleId><ArticleId IdType="doi">10.7717/peerj.4665</ArticleId><ArticleId IdType="pii">4665</ArticleId><ArticleId IdType="pmc">PMC5909683</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Bioinformatics. 2006 Nov 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Mullendore</name></region><name sortKey="Hellmann, Hanjo H" sort="Hellmann, Hanjo H" uniqKey="Hellmann H" first="Hanjo H" last="Hellmann">Hanjo H. Hellmann</name><name sortKey="Knoblauch, Michael" sort="Knoblauch, Michael" uniqKey="Knoblauch M" first="Michael" last="Knoblauch">Michael Knoblauch</name><name sortKey="Liu, Yan" sort="Liu, Yan" uniqKey="Liu Y" first="Yan" last="Liu">Yan Liu</name><name sortKey="Peters, Winfried S" sort="Peters, Winfried S" uniqKey="Peters W" first="Winfried S" last="Peters">Winfried S. Peters</name><name sortKey="Roalson, Eric H" sort="Roalson, Eric H" uniqKey="Roalson E" first="Eric H" last="Roalson">Eric H. Roalson</name><name sortKey="Ross Elliott, Timothy" sort="Ross Elliott, Timothy" uniqKey="Ross Elliott T" first="Timothy" last="Ross-Elliott">Timothy Ross-Elliott</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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