Characterization and ectopic expression of a populus hydroxyacid hydroxycinnamoyltransferase.
Identifieur interne : 002769 ( Main/Exploration ); précédent : 002768; suivant : 002770Characterization and ectopic expression of a populus hydroxyacid hydroxycinnamoyltransferase.
Auteurs : Ai-Xia Cheng [États-Unis] ; Jin-Ying Gou ; Xiao-Hong Yu ; Huijun Yang ; Xin Fang ; Xiao-Ya Chen ; Chang-Jun LiuSource :
- Molecular plant [ 1752-9867 ] ; 2013.
Descripteurs français
- KwdFr :
- Acyltransferases (métabolisme), Adaptation physiologique (MeSH), Chlorure de sodium (MeSH), Données de séquences moléculaires (MeSH), Feuilles de plante (enzymologie), Graines (enzymologie), Phylogenèse (MeSH), Populus (classification), Populus (embryologie), Populus (enzymologie), Protéines recombinantes (métabolisme), Protéines végétales (métabolisme), Racines de plante (enzymologie).
- MESH :
- embryologie : Populus.
- enzymologie : Feuilles de plante, Graines, Populus, Racines de plante.
- métabolisme : Acyltransferases, Populus, Protéines recombinantes, Protéines végétales.
- Adaptation physiologique, Chlorure de sodium, Données de séquences moléculaires, Phylogenèse.
English descriptors
- KwdEn :
- Acyltransferases (metabolism), Adaptation, Physiological (MeSH), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Plant Leaves (enzymology), Plant Proteins (metabolism), Plant Roots (enzymology), Populus (classification), Populus (embryology), Populus (enzymology), Recombinant Proteins (metabolism), Seeds (enzymology), Sodium Chloride (MeSH).
- MESH :
- chemical , metabolism : Acyltransferases, Plant Proteins, Recombinant Proteins.
- classification : Populus.
- embryology : Populus.
- enzymology : Plant Leaves, Plant Roots, Populus, Seeds.
- Adaptation, Physiological, Molecular Sequence Data, Phylogeny, Sodium Chloride.
Abstract
Cutinized and suberized cell walls in plants constitute physiologically important environment interfaces. They act as barriers limiting the loss of water and nutrients and protecting against radiation and invasion of pathogens. The roles of cutin- and suberin polyesters are often attributed to their dominant aliphatic components, but the contribution of aromatic composition to their physiological function remains unclear. By functionally screening a subset of Populus trichocarpa BAHD/HXXXD acyltransferases, we identified a hydroxycinnamoyltransferase that shows specific transacylation activity on ω-hydroxyacids using both feruloyl- and p-coumaroyl- CoA as the acyl donors. We named this enzyme P. trichocarpa hydroxyacid/fatty alcohol hydroxycinnamoyltransferase 1 (PtFHT1). The ectopic expression of the PtFHT1 gene in Arabidopsis increased the incorporation of ferulate in root and seed suberins and in leaf cutin, but not that of p-coumarate, while the aliphatic load in both suberin and cutin polyesters essentially remained unaffected. The overaccumulation of ferulate in lipophilic polyester significantly increased the tolerance of transgenic plants to salt stress treatment; under sub-lethal conditions of salt stress, the ratios of their seed germination and seedling establishment were 50% higher than those of wild-type plants. Our study suggests that, although aromatics are the minor component of polyesters, they play important role in the sealing function of lipidic polymers in planta.
DOI: 10.1093/mp/sst085
PubMed: 23709341
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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uniqKey="Yang H" first="Huijun" last="Yang">Huijun Yang</name></author><author><name sortKey="Fang, Xin" sort="Fang, Xin" uniqKey="Fang X" first="Xin" last="Fang">Xin Fang</name></author><author><name sortKey="Chen, Xiao Ya" sort="Chen, Xiao Ya" uniqKey="Chen X" first="Xiao-Ya" last="Chen">Xiao-Ya Chen</name></author><author><name sortKey="Liu, Chang Jun" sort="Liu, Chang Jun" uniqKey="Liu C" first="Chang-Jun" last="Liu">Chang-Jun Liu</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23709341</idno><idno type="pmid">23709341</idno><idno type="doi">10.1093/mp/sst085</idno><idno type="wicri:Area/Main/Corpus">002579</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002579</idno><idno type="wicri:Area/Main/Curation">002579</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002579</idno><idno 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Yu</name></author><author><name sortKey="Yang, Huijun" sort="Yang, Huijun" uniqKey="Yang H" first="Huijun" last="Yang">Huijun Yang</name></author><author><name sortKey="Fang, Xin" sort="Fang, Xin" uniqKey="Fang X" first="Xin" last="Fang">Xin Fang</name></author><author><name sortKey="Chen, Xiao Ya" sort="Chen, Xiao Ya" uniqKey="Chen X" first="Xiao-Ya" last="Chen">Xiao-Ya Chen</name></author><author><name sortKey="Liu, Chang Jun" sort="Liu, Chang Jun" uniqKey="Liu C" first="Chang-Jun" last="Liu">Chang-Jun Liu</name></author></analytic><series><title level="j">Molecular plant</title><idno type="eISSN">1752-9867</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acyltransferases (metabolism)</term><term>Adaptation, Physiological (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phylogeny (MeSH)</term><term>Plant Leaves (enzymology)</term><term>Plant Proteins (metabolism)</term><term>Plant Roots (enzymology)</term><term>Populus (classification)</term><term>Populus (embryology)</term><term>Populus (enzymology)</term><term>Recombinant Proteins (metabolism)</term><term>Seeds (enzymology)</term><term>Sodium Chloride (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acyltransferases (métabolisme)</term><term>Adaptation physiologique (MeSH)</term><term>Chlorure de sodium (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Feuilles de plante (enzymologie)</term><term>Graines (enzymologie)</term><term>Phylogenèse (MeSH)</term><term>Populus (classification)</term><term>Populus (embryologie)</term><term>Populus (enzymologie)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (métabolisme)</term><term>Racines de plante (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acyltransferases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="embryologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="embryology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Feuilles de plante</term><term>Graines</term><term>Populus</term><term>Racines de plante</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plant Leaves</term><term>Plant Roots</term><term>Populus</term><term>Seeds</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acyltransferases</term><term>Populus</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adaptation, Physiological</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Sodium Chloride</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adaptation physiologique</term><term>Chlorure de sodium</term><term>Données de séquences moléculaires</term><term>Phylogenèse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cutinized and suberized cell walls in plants constitute physiologically important environment interfaces. They act as barriers limiting the loss of water and nutrients and protecting against radiation and invasion of pathogens. The roles of cutin- and suberin polyesters are often attributed to their dominant aliphatic components, but the contribution of aromatic composition to their physiological function remains unclear. By functionally screening a subset of Populus trichocarpa BAHD/HXXXD acyltransferases, we identified a hydroxycinnamoyltransferase that shows specific transacylation activity on ω-hydroxyacids using both feruloyl- and p-coumaroyl- CoA as the acyl donors. We named this enzyme P. trichocarpa hydroxyacid/fatty alcohol hydroxycinnamoyltransferase 1 (PtFHT1). The ectopic expression of the PtFHT1 gene in Arabidopsis increased the incorporation of ferulate in root and seed suberins and in leaf cutin, but not that of p-coumarate, while the aliphatic load in both suberin and cutin polyesters essentially remained unaffected. The overaccumulation of ferulate in lipophilic polyester significantly increased the tolerance of transgenic plants to salt stress treatment; under sub-lethal conditions of salt stress, the ratios of their seed germination and seedling establishment were 50% higher than those of wild-type plants. Our study suggests that, although aromatics are the minor component of polyesters, they play important role in the sealing function of lipidic polymers in planta. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23709341</PMID><DateCompleted><Year>2014</Year><Month>05</Month><Day>22</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1752-9867</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><Issue>6</Issue><PubDate><Year>2013</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Molecular plant</Title><ISOAbbreviation>Mol Plant</ISOAbbreviation></Journal><ArticleTitle>Characterization and ectopic expression of a populus hydroxyacid hydroxycinnamoyltransferase.</ArticleTitle><Pagination><MedlinePgn>1889-903</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/mp/sst085</ELocationID><Abstract><AbstractText>Cutinized and suberized cell walls in plants constitute physiologically important environment interfaces. They act as barriers limiting the loss of water and nutrients and protecting against radiation and invasion of pathogens. The roles of cutin- and suberin polyesters are often attributed to their dominant aliphatic components, but the contribution of aromatic composition to their physiological function remains unclear. By functionally screening a subset of Populus trichocarpa BAHD/HXXXD acyltransferases, we identified a hydroxycinnamoyltransferase that shows specific transacylation activity on ω-hydroxyacids using both feruloyl- and p-coumaroyl- CoA as the acyl donors. We named this enzyme P. trichocarpa hydroxyacid/fatty alcohol hydroxycinnamoyltransferase 1 (PtFHT1). The ectopic expression of the PtFHT1 gene in Arabidopsis increased the incorporation of ferulate in root and seed suberins and in leaf cutin, but not that of p-coumarate, while the aliphatic load in both suberin and cutin polyesters essentially remained unaffected. The overaccumulation of ferulate in lipophilic polyester significantly increased the tolerance of transgenic plants to salt stress treatment; under sub-lethal conditions of salt stress, the ratios of their seed germination and seedling establishment were 50% higher than those of wild-type plants. Our study suggests that, although aromatics are the minor component of polyesters, they play important role in the sealing function of lipidic polymers in planta. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cheng</LastName><ForeName>Ai-Xia</ForeName><Initials>AX</Initials><AffiliationInfo><Affiliation>Biosciences Department, Brookhaven National Laboratory, Upton, NY 11973, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gou</LastName><ForeName>Jin-Ying</ForeName><Initials>JY</Initials></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Xiao-Hong</ForeName><Initials>XH</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Huijun</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Fang</LastName><ForeName>Xin</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Xiao-Ya</ForeName><Initials>XY</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Chang-Jun</ForeName><Initials>CJ</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>JX515962</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>05</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Mol Plant</MedlineTA><NlmUniqueID>101465514</NlmUniqueID><ISSNLinking>1674-2052</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Seeds</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012965" MajorTopicYN="N">Sodium Chloride</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">BAHD</Keyword><Keyword MajorTopicYN="N">Populus.</Keyword><Keyword MajorTopicYN="N">acyltransferase</Keyword><Keyword MajorTopicYN="N">cutin</Keyword><Keyword MajorTopicYN="N">ferulate</Keyword><Keyword MajorTopicYN="N">suberin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>5</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>5</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>5</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23709341</ArticleId><ArticleId IdType="pii">S1674-2052(14)60271-9</ArticleId><ArticleId IdType="doi">10.1093/mp/sst085</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><noCountry><name sortKey="Chen, Xiao Ya" sort="Chen, Xiao Ya" uniqKey="Chen X" first="Xiao-Ya" last="Chen">Xiao-Ya Chen</name><name sortKey="Fang, Xin" sort="Fang, Xin" uniqKey="Fang X" first="Xin" last="Fang">Xin Fang</name><name sortKey="Gou, Jin Ying" sort="Gou, Jin Ying" uniqKey="Gou J" first="Jin-Ying" last="Gou">Jin-Ying Gou</name><name sortKey="Liu, Chang Jun" sort="Liu, Chang Jun" uniqKey="Liu C" first="Chang-Jun" last="Liu">Chang-Jun Liu</name><name sortKey="Yang, Huijun" sort="Yang, Huijun" uniqKey="Yang H" first="Huijun" last="Yang">Huijun Yang</name><name sortKey="Yu, Xiao Hong" sort="Yu, Xiao Hong" uniqKey="Yu X" first="Xiao-Hong" last="Yu">Xiao-Hong Yu</name></noCountry><country name="États-Unis"><region name="État de New York"><name sortKey="Cheng, Ai Xia" sort="Cheng, Ai Xia" uniqKey="Cheng A" first="Ai-Xia" last="Cheng">Ai-Xia Cheng</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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