Heterologous expression and functional characterization of two hybrid poplar cell-wall invertases.
Identifieur interne : 003897 ( Main/Exploration ); précédent : 003896; suivant : 003898Heterologous expression and functional characterization of two hybrid poplar cell-wall invertases.
Auteurs : Thomas Canam [Canada] ; Faride Unda ; Shawn D. MansfieldSource :
- Planta [ 0032-0935 ] ; 2008.
Descripteurs français
- KwdFr :
- Cations (pharmacologie), Concentration en ions d'hydrogène (MeSH), Hybridation génétique (MeSH), Modèles moléculaires (MeSH), Motifs d'acides aminés (MeSH), Paroi cellulaire (enzymologie), Pichia (génétique), Populus (croissance et développement), Populus (enzymologie), Populus (génétique), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (métabolisme), Protéines végétales (physiologie), Spécificité du substrat (MeSH), Stabilité enzymatique (effets des médicaments et des substances chimiques), Structure tertiaire des protéines (MeSH), Température (MeSH), beta-Fructofuranosidase (composition chimique), beta-Fructofuranosidase (génétique), beta-Fructofuranosidase (métabolisme), beta-Fructofuranosidase (physiologie).
- MESH :
- composition chimique : Protéines végétales, beta-Fructofuranosidase.
- croissance et développement : Populus.
- effets des médicaments et des substances chimiques : Stabilité enzymatique.
- enzymologie : Paroi cellulaire, Populus.
- génétique : Pichia, Populus, Protéines végétales, beta-Fructofuranosidase.
- métabolisme : Protéines végétales, beta-Fructofuranosidase.
- pharmacologie : Cations.
- physiologie : Protéines végétales, beta-Fructofuranosidase.
- Concentration en ions d'hydrogène, Hybridation génétique, Modèles moléculaires, Motifs d'acides aminés, Spécificité du substrat, Structure tertiaire des protéines, Température.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Cations (pharmacology), Cell Wall (enzymology), Enzyme Stability (drug effects), Hybridization, Genetic (MeSH), Hydrogen-Ion Concentration (MeSH), Models, Molecular (MeSH), Pichia (genetics), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Plant Proteins (physiology), Populus (enzymology), Populus (genetics), Populus (growth & development), Protein Structure, Tertiary (MeSH), Substrate Specificity (MeSH), Temperature (MeSH), beta-Fructofuranosidase (chemistry), beta-Fructofuranosidase (genetics), beta-Fructofuranosidase (metabolism), beta-Fructofuranosidase (physiology).
- MESH :
- chemical , chemistry : Plant Proteins, beta-Fructofuranosidase.
- chemical , genetics : Plant Proteins, beta-Fructofuranosidase.
- chemical , metabolism : Plant Proteins, beta-Fructofuranosidase.
- chemical , pharmacology : Cations.
- drug effects : Enzyme Stability.
- enzymology : Cell Wall, Populus.
- genetics : Pichia, Populus.
- growth & development : Populus.
- chemical , physiology : Plant Proteins, beta-Fructofuranosidase.
- Amino Acid Motifs, Hybridization, Genetic, Hydrogen-Ion Concentration, Models, Molecular, Protein Structure, Tertiary, Substrate Specificity, Temperature.
Abstract
The expression of two hybrid poplar cell-wall invertases (EC 3.2.1.26; PaxgINV1 and PaxgINV2) were previously shown to be spatially and temporally regulated in the vegetative tissues. The expression of PaxgINV1 was linked to processes relating to dormancy, while PaxgINV2 expression was prominent in tissues undergoing growth and expansion. In an effort to further elucidate the physiological roles of these key cell wall enzymes, PaxgINV1 and PaxgINV2 were heterologously expressed in the methylotrophic yeast Pichia pastoris. Three-dimensional predictive models of the poplar invertases revealed a structural channel containing both the conserved beta-fructofuranosidase and cell-wall invertase motifs, suggesting that this channel is the putative active site of these enzymes. Recombinant PaxgINV1 and PaxgINV2 had pH optima of 4.8 and 5.6 and temperature optima of 45 and 40 degrees C, respectively. Functional characterization revealed the ability for both enzymes to hydrolyze the fructose residue of sucrose, raffinose, stachyose and verbascose, with PaxgINV2 having higher specific activity for each of the substrates tested. The K(m) values of sucrose/raffinose/stachyose were 1.7/1.8/5.0 mM for PaxgINV1 and 1.6/1.7/1.9 mM for PaxgINV2, respectively. Activity analyses in the presence of various metal cations showed that PaxgINV2 was strongly inhibited by Cu(2+), Zn(2+) and Hg(2+), while PaxgINV1 was only weakly inhibited by these cations. The results from this study, coupled with previous expression data, suggest that PaxgINV1 and PaxgINV2 have distinct roles with respect to the physiology and development of hybrid poplar, specifically phloem unloading and processes related to dormancy and bud break.
DOI: 10.1007/s00425-008-0801-6
PubMed: 18704491
Affiliations:
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génétique</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Spécificité du substrat</term><term>Structure tertiaire des protéines</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The expression of two hybrid poplar cell-wall invertases (EC 3.2.1.26; PaxgINV1 and PaxgINV2) were previously shown to be spatially and temporally regulated in the vegetative tissues. The expression of PaxgINV1 was linked to processes relating to dormancy, while PaxgINV2 expression was prominent in tissues undergoing growth and expansion. In an effort to further elucidate the physiological roles of these key cell wall enzymes, PaxgINV1 and PaxgINV2 were heterologously expressed in the methylotrophic yeast Pichia pastoris. Three-dimensional predictive models of the poplar invertases revealed a structural channel containing both the conserved beta-fructofuranosidase and cell-wall invertase motifs, suggesting that this channel is the putative active site of these enzymes. Recombinant PaxgINV1 and PaxgINV2 had pH optima of 4.8 and 5.6 and temperature optima of 45 and 40 degrees C, respectively. Functional characterization revealed the ability for both enzymes to hydrolyze the fructose residue of sucrose, raffinose, stachyose and verbascose, with PaxgINV2 having higher specific activity for each of the substrates tested. The K(m) values of sucrose/raffinose/stachyose were 1.7/1.8/5.0 mM for PaxgINV1 and 1.6/1.7/1.9 mM for PaxgINV2, respectively. Activity analyses in the presence of various metal cations showed that PaxgINV2 was strongly inhibited by Cu(2+), Zn(2+) and Hg(2+), while PaxgINV1 was only weakly inhibited by these cations. The results from this study, coupled with previous expression data, suggest that PaxgINV1 and PaxgINV2 have distinct roles with respect to the physiology and development of hybrid poplar, specifically phloem unloading and processes related to dormancy and bud break.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18704491</PMID><DateCompleted><Year>2009</Year><Month>03</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0032-0935</ISSN><JournalIssue CitedMedium="Print"><Volume>228</Volume><Issue>6</Issue><PubDate><Year>2008</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Heterologous expression and functional characterization of two hybrid poplar cell-wall invertases.</ArticleTitle><Pagination><MedlinePgn>1011-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00425-008-0801-6</ELocationID><Abstract><AbstractText>The expression of two hybrid poplar cell-wall invertases (EC 3.2.1.26; PaxgINV1 and PaxgINV2) were previously shown to be spatially and temporally regulated in the vegetative tissues. The expression of PaxgINV1 was linked to processes relating to dormancy, while PaxgINV2 expression was prominent in tissues undergoing growth and expansion. In an effort to further elucidate the physiological roles of these key cell wall enzymes, PaxgINV1 and PaxgINV2 were heterologously expressed in the methylotrophic yeast Pichia pastoris. Three-dimensional predictive models of the poplar invertases revealed a structural channel containing both the conserved beta-fructofuranosidase and cell-wall invertase motifs, suggesting that this channel is the putative active site of these enzymes. Recombinant PaxgINV1 and PaxgINV2 had pH optima of 4.8 and 5.6 and temperature optima of 45 and 40 degrees C, respectively. Functional characterization revealed the ability for both enzymes to hydrolyze the fructose residue of sucrose, raffinose, stachyose and verbascose, with PaxgINV2 having higher specific activity for each of the substrates tested. The K(m) values of sucrose/raffinose/stachyose were 1.7/1.8/5.0 mM for PaxgINV1 and 1.6/1.7/1.9 mM for PaxgINV2, respectively. Activity analyses in the presence of various metal cations showed that PaxgINV2 was strongly inhibited by Cu(2+), Zn(2+) and Hg(2+), while PaxgINV1 was only weakly inhibited by these cations. The results from this study, coupled with previous expression data, suggest that PaxgINV1 and PaxgINV2 have distinct roles with respect to the physiology and development of hybrid poplar, specifically phloem unloading and processes related to dormancy and bud break.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Canam</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Wood Science, University of British Columbia, Vancouver, BC, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Unda</LastName><ForeName>Faride</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Mansfield</LastName><ForeName>Shawn D</ForeName><Initials>SD</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>2008</Year><Month>08</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002412">Cations</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.26</RegistryNumber><NameOfSubstance UI="D043324">beta-Fructofuranosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002412" MajorTopicYN="N">Cations</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006824" MajorTopicYN="N">Hybridization, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D043324" MajorTopicYN="N">beta-Fructofuranosidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2008</Year><Month>06</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2008</Year><Month>07</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>8</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>3</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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</li></region><settlement><li>Vancouver</li></settlement><orgName><li>Université de la Colombie-Britannique</li></orgName></list><tree><noCountry><name sortKey="Mansfield, Shawn D" sort="Mansfield, Shawn D" uniqKey="Mansfield S" first="Shawn D" last="Mansfield">Shawn D. Mansfield</name><name sortKey="Unda, Faride" sort="Unda, Faride" uniqKey="Unda F" first="Faride" last="Unda">Faride Unda</name></noCountry><country name="Canada"><region name="Colombie-Britannique "><name sortKey="Canam, Thomas" sort="Canam, Thomas" uniqKey="Canam T" first="Thomas" last="Canam">Thomas Canam</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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