Proteomic analysis of hybrid poplar xylem sap.
Identifieur interne : 003513 ( Main/Exploration ); précédent : 003512; suivant : 003514Proteomic analysis of hybrid poplar xylem sap.
Auteurs : Nicole J. Dafoe [Canada] ; C Peter ConstabelSource :
- Phytochemistry [ 1873-3700 ] ; 2009.
Descripteurs français
- KwdFr :
- MESH :
- analyse : Protéines végétales.
- composition chimique : Populus, Racines de plante, Xylème.
- métabolisme : Protéines végétales, Xylème.
- Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Plant Proteins.
- chemical , metabolism : Plant Proteins.
- chemistry : Plant Roots, Populus, Xylem.
- metabolism : Xylem.
- Electrophoresis, Polyacrylamide Gel.
Abstract
Xylem sap collected from Populus trichocarpaxPopulus deltoides using root pressure was estimated to contain more than 100 proteins. Ninety-seven of these proteins were identified using liquid chromatography-tandem mass spectrometry (LC-MS/MS). These proteins were classified into 10 functional categories including metabolism, signaling, stress response and cell wall functions. The majority of xylem sap proteins were metabolic enzymes involved in processes including translation, proteolysis, and glycolysis. Stress-related proteins were also prevalent. In contrast to xylem sap proteins collected from annual plants, the majority of poplar xylem sap proteins do not appear to be classically secreted since only 33 proteins were predicted to have an N-terminal signal peptide targeting them to the secretory pathway. Of the remaining 64 proteins, 27 were predicted to be secreted non-classically. While a number of proteins identified here have been previously reported in xylem sap proteomes of annual plants, many xylem sap proteins were identified in poplar which may reflect functions specific to perennial plants.
DOI: 10.1016/j.phytochem.2009.04.016
PubMed: 19467552
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Dafoe</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Forest Biology and Department of Biology, P.O. Box 3020, Station CSC, Victoria, Canada BC V8W 3N5.</nlm:affiliation><country>Canada</country><wicri:regionArea>Centre for Forest Biology and Department of Biology, P.O. 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Ninety-seven of these proteins were identified using liquid chromatography-tandem mass spectrometry (LC-MS/MS). These proteins were classified into 10 functional categories including metabolism, signaling, stress response and cell wall functions. The majority of xylem sap proteins were metabolic enzymes involved in processes including translation, proteolysis, and glycolysis. Stress-related proteins were also prevalent. In contrast to xylem sap proteins collected from annual plants, the majority of poplar xylem sap proteins do not appear to be classically secreted since only 33 proteins were predicted to have an N-terminal signal peptide targeting them to the secretory pathway. Of the remaining 64 proteins, 27 were predicted to be secreted non-classically. While a number of proteins identified here have been previously reported in xylem sap proteomes of annual plants, many xylem sap proteins were identified in poplar which may reflect functions specific to perennial plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19467552</PMID><DateCompleted><Year>2009</Year><Month>07</Month><Day>09</Day></DateCompleted><DateRevised><Year>2009</Year><Month>06</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3700</ISSN><JournalIssue CitedMedium="Internet"><Volume>70</Volume><Issue>7</Issue><PubDate><Year>2009</Year><Month>May</Month></PubDate></JournalIssue><Title>Phytochemistry</Title><ISOAbbreviation>Phytochemistry</ISOAbbreviation></Journal><ArticleTitle>Proteomic analysis of hybrid poplar xylem sap.</ArticleTitle><Pagination><MedlinePgn>856-63</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.phytochem.2009.04.016</ELocationID><Abstract><AbstractText>Xylem sap collected from Populus trichocarpaxPopulus deltoides using root pressure was estimated to contain more than 100 proteins. Ninety-seven of these proteins were identified using liquid chromatography-tandem mass spectrometry (LC-MS/MS). These proteins were classified into 10 functional categories including metabolism, signaling, stress response and cell wall functions. The majority of xylem sap proteins were metabolic enzymes involved in processes including translation, proteolysis, and glycolysis. Stress-related proteins were also prevalent. In contrast to xylem sap proteins collected from annual plants, the majority of poplar xylem sap proteins do not appear to be classically secreted since only 33 proteins were predicted to have an N-terminal signal peptide targeting them to the secretory pathway. Of the remaining 64 proteins, 27 were predicted to be secreted non-classically. While a number of proteins identified here have been previously reported in xylem sap proteomes of annual plants, many xylem sap proteins were identified in poplar which may reflect functions specific to perennial plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dafoe</LastName><ForeName>Nicole J</ForeName><Initials>NJ</Initials><AffiliationInfo><Affiliation>Centre for Forest Biology and Department of Biology, P.O. Box 3020, Station CSC, Victoria, Canada BC V8W 3N5.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Constabel</LastName><ForeName>C Peter</ForeName><Initials>CP</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>05</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Phytochemistry</MedlineTA><NlmUniqueID>0151434</NlmUniqueID><ISSNLinking>0031-9422</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018517" MajorTopicYN="N">Plant Roots</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D052584" MajorTopicYN="N">Xylem</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>01</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2009</Year><Month>04</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>04</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>5</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>5</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>7</Month><Day>10</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19467552</ArticleId><ArticleId IdType="pii">S0031-9422(09)00168-X</ArticleId><ArticleId IdType="doi">10.1016/j.phytochem.2009.04.016</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Constabel, C Peter" sort="Constabel, C Peter" uniqKey="Constabel C" first="C Peter" last="Constabel">C Peter Constabel</name></noCountry><country name="Canada"><noRegion><name sortKey="Dafoe, Nicole J" sort="Dafoe, Nicole J" uniqKey="Dafoe N" first="Nicole J" last="Dafoe">Nicole J. 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