Regulation of phenylalanine ammonia-lyase (PAL) gene family in wood forming tissue of Populus trichocarpa.
Identifieur interne : 002506 ( Main/Exploration ); précédent : 002505; suivant : 002507Regulation of phenylalanine ammonia-lyase (PAL) gene family in wood forming tissue of Populus trichocarpa.
Auteurs : Rui Shi [États-Unis] ; Christopher M. Shuford ; Jack P. Wang ; Ying-Hsuan Sun ; Zhichang Yang ; Hsi-Chuan Chen ; Sermsawat Tunlaya-Anukit ; Quanzi Li ; Jie Liu ; David C. Muddiman ; Ronald R. Sederoff ; Vincent L. ChiangSource :
- Planta [ 1432-2048 ] ; 2013.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Populus.
- métabolisme : Phenylalanine ammonia-lyase, Populus.
- physiologie : Régulation de l'expression des gènes végétaux.
- Spectrométrie de masse.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Phenylalanine Ammonia-Lyase.
- enzymology : Populus.
- metabolism : Populus.
- physiology : Gene Expression Regulation, Plant.
- Mass Spectrometry.
Abstract
Phenylalanine ammonia-lyase (PAL) catalyzes the initial step of phenylpropanoid biosynthesis in plants. Five PAL genes (PtrPAL1 to 5) have been identified in Populus trichocarpa. These genes are classified into two subgroups according to their transcript sequence similarity and tissue specificity. However, the regulation of these genes and their protein functions are not well understood. In this study, enzymatic properties of each PtrPALs were characterized based on their recombinant proteins expressed in E.coli. Subcellular localizations of each PtrPALs in stem wood forming tissue were investigated and individual PtrPAL protein abundances in cytosol and membrane protein fractions were measured using protein cleavage-isotope dilution mass spectrometry (PC-IDMS). Protein/mRNA ratios of PtrPALs were further verified using RNA-Seq and gel-enhanced liquid chromatography mass spectrometry (GeLC-MS). All PtrPALs have similar catalytic properties for the deamination of L-phenylalanine, their major substrate. All PtrPALs have similar subcellular locations in stem wood forming tissue, with major amount in the cytosol (93-96 %) and less in the membrane (4-7 %). However, the protein/mRNA ratios of subgroup A (PtrPAL2, 4 and 5) are about five times that of subgroup B (PtrPAL1 and 3) in stem wood forming tissue, while all PtrPALs have similar transcript abundances. These results indicate a greater functional significance of subgroup A PtrPALs for stem wood formation, and highlight the role of gene post-transcriptional regulation.
DOI: 10.1007/s00425-013-1905-1
PubMed: 23765265
Affiliations:
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Muddiman</name></author><author><name sortKey="Sederoff, Ronald R" sort="Sederoff, Ronald R" uniqKey="Sederoff R" first="Ronald R" last="Sederoff">Ronald R. Sederoff</name></author><author><name sortKey="Chiang, Vincent L" sort="Chiang, Vincent L" uniqKey="Chiang V" first="Vincent L" last="Chiang">Vincent L. Chiang</name></author></analytic><series><title level="j">Planta</title><idno type="eISSN">1432-2048</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Gene Expression Regulation, Plant (physiology)</term><term>Mass Spectrometry (MeSH)</term><term>Phenylalanine Ammonia-Lyase (metabolism)</term><term>Populus (enzymology)</term><term>Populus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Phenylalanine ammonia-lyase (métabolisme)</term><term>Populus (enzymologie)</term><term>Populus (métabolisme)</term><term>Régulation de l'expression des gènes végétaux (physiologie)</term><term>Spectrométrie de masse (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Phenylalanine Ammonia-Lyase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phenylalanine ammonia-lyase</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Régulation de l'expression des gènes végétaux</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Plant</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Mass Spectrometry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Spectrométrie de masse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Phenylalanine ammonia-lyase (PAL) catalyzes the initial step of phenylpropanoid biosynthesis in plants. Five PAL genes (PtrPAL1 to 5) have been identified in Populus trichocarpa. These genes are classified into two subgroups according to their transcript sequence similarity and tissue specificity. However, the regulation of these genes and their protein functions are not well understood. In this study, enzymatic properties of each PtrPALs were characterized based on their recombinant proteins expressed in E.coli. Subcellular localizations of each PtrPALs in stem wood forming tissue were investigated and individual PtrPAL protein abundances in cytosol and membrane protein fractions were measured using protein cleavage-isotope dilution mass spectrometry (PC-IDMS). Protein/mRNA ratios of PtrPALs were further verified using RNA-Seq and gel-enhanced liquid chromatography mass spectrometry (GeLC-MS). All PtrPALs have similar catalytic properties for the deamination of L-phenylalanine, their major substrate. All PtrPALs have similar subcellular locations in stem wood forming tissue, with major amount in the cytosol (93-96 %) and less in the membrane (4-7 %). However, the protein/mRNA ratios of subgroup A (PtrPAL2, 4 and 5) are about five times that of subgroup B (PtrPAL1 and 3) in stem wood forming tissue, while all PtrPALs have similar transcript abundances. These results indicate a greater functional significance of subgroup A PtrPALs for stem wood formation, and highlight the role of gene post-transcriptional regulation. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23765265</PMID><DateCompleted><Year>2014</Year><Month>03</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-2048</ISSN><JournalIssue CitedMedium="Internet"><Volume>238</Volume><Issue>3</Issue><PubDate><Year>2013</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Regulation of phenylalanine ammonia-lyase (PAL) gene family in wood forming tissue of Populus trichocarpa.</ArticleTitle><Pagination><MedlinePgn>487-97</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00425-013-1905-1</ELocationID><Abstract><AbstractText>Phenylalanine ammonia-lyase (PAL) catalyzes the initial step of phenylpropanoid biosynthesis in plants. Five PAL genes (PtrPAL1 to 5) have been identified in Populus trichocarpa. These genes are classified into two subgroups according to their transcript sequence similarity and tissue specificity. However, the regulation of these genes and their protein functions are not well understood. In this study, enzymatic properties of each PtrPALs were characterized based on their recombinant proteins expressed in E.coli. Subcellular localizations of each PtrPALs in stem wood forming tissue were investigated and individual PtrPAL protein abundances in cytosol and membrane protein fractions were measured using protein cleavage-isotope dilution mass spectrometry (PC-IDMS). Protein/mRNA ratios of PtrPALs were further verified using RNA-Seq and gel-enhanced liquid chromatography mass spectrometry (GeLC-MS). All PtrPALs have similar catalytic properties for the deamination of L-phenylalanine, their major substrate. All PtrPALs have similar subcellular locations in stem wood forming tissue, with major amount in the cytosol (93-96 %) and less in the membrane (4-7 %). However, the protein/mRNA ratios of subgroup A (PtrPAL2, 4 and 5) are about five times that of subgroup B (PtrPAL1 and 3) in stem wood forming tissue, while all PtrPALs have similar transcript abundances. These results indicate a greater functional significance of subgroup A PtrPALs for stem wood formation, and highlight the role of gene post-transcriptional regulation. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shi</LastName><ForeName>Rui</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695, USA. rshi@ncsu.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shuford</LastName><ForeName>Christopher M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Jack P</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Ying-Hsuan</ForeName><Initials>YH</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Zhichang</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Hsi-Chuan</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Tunlaya-Anukit</LastName><ForeName>Sermsawat</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Quanzi</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Jie</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Muddiman</LastName><ForeName>David C</ForeName><Initials>DC</Initials></Author><Author ValidYN="Y"><LastName>Sederoff</LastName><ForeName>Ronald R</ForeName><Initials>RR</Initials></Author><Author ValidYN="Y"><LastName>Chiang</LastName><ForeName>Vincent L</ForeName><Initials>VL</Initials></Author></AuthorList><Language>eng</Language><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>06</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 4.3.1.24</RegistryNumber><NameOfSubstance UI="D010650">Phenylalanine Ammonia-Lyase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010650" MajorTopicYN="N">Phenylalanine Ammonia-Lyase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>04</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>05</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>6</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>6</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>3</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23765265</ArticleId><ArticleId 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Shuford</name><name sortKey="Sun, Ying Hsuan" sort="Sun, Ying Hsuan" uniqKey="Sun Y" first="Ying-Hsuan" last="Sun">Ying-Hsuan Sun</name><name sortKey="Tunlaya Anukit, Sermsawat" sort="Tunlaya Anukit, Sermsawat" uniqKey="Tunlaya Anukit S" first="Sermsawat" last="Tunlaya-Anukit">Sermsawat Tunlaya-Anukit</name><name sortKey="Wang, Jack P" sort="Wang, Jack P" uniqKey="Wang J" first="Jack P" last="Wang">Jack P. Wang</name><name sortKey="Yang, Zhichang" sort="Yang, Zhichang" uniqKey="Yang Z" first="Zhichang" last="Yang">Zhichang Yang</name></noCountry><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Shi, Rui" sort="Shi, Rui" uniqKey="Shi R" first="Rui" last="Shi">Rui Shi</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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