Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation.
Identifieur interne : 001B27 ( Main/Exploration ); précédent : 001B26; suivant : 001B28Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation.
Auteurs : Victoria J. Maloney [Canada] ; Ji-Young Park [Canada] ; Faride Unda [Canada] ; Shawn D. Mansfield [Canada]Source :
- Journal of experimental botany [ 1460-2431 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
- croissance et développement : Arabidopsis.
- enzymologie : Arabidopsis.
- métabolisme : Arabidopsis, Glucosyltransferases, Phosphoprotein Phosphatases, Plantes.
- Biomasse, Liaison aux protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glucosyltransferases, Phosphoprotein Phosphatases.
- enzymology : Arabidopsis.
- growth & development : Arabidopsis.
- metabolism : Arabidopsis, Plants.
- Biomass, Protein Binding.
Abstract
Bioinformatic analysis indicates that sucrose phosphate synthase (SPS) contains a putative C-terminal sucrose phosphate phosphatase (SPP)-like domain that may facilitates the binding of SPP. If an SPS-SPP enzyme complex exists, it may provide sucrose biosynthesis with an additional level of regulation, forming a direct metabolic channel for sucrose-6-phosphate between these two enzymes. Herein, the formation of an enzyme complex between SPS and SPP was examined, and the results from yeast two-hybrid experiments suggest that there is indeed an association between these proteins. In addition, in planta bioluminescence resonance energy transfer (BRET) was observed in Arabidopsis seedlings, providing physical evidence for a protein interaction in live cells and in real time. Finally, bimolecular fluorescence complementation (BiFC) was employed in an attempt to detect SPS-SPP interactions visually. The findings clearly demonstrated that SPS interacts with SPP and that this interaction impacts soluble carbohydrate pools and affects carbon partitioning to starch. Moreover, a fusion construct between the two genes promotes plant growth in both transgenic Arabidopsis and hybrid poplar.
DOI: 10.1093/jxb/erv101
PubMed: 25873678
PubMed Central: PMC4493782
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Maloney</name><affiliation wicri:level="4"><nlm:affiliation>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4</wicri:regionArea><orgName type="university">Université de la Colombie-Britannique</orgName><placeName><settlement type="city">Vancouver</settlement><region type="state">Colombie-Britannique </region></placeName></affiliation></author><author><name sortKey="Park, Ji Young" sort="Park, Ji Young" uniqKey="Park J" first="Ji-Young" last="Park">Ji-Young Park</name><affiliation wicri:level="4"><nlm:affiliation>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4</wicri:regionArea><orgName type="university">Université de la Colombie-Britannique</orgName><placeName><settlement type="city">Vancouver</settlement><region type="state">Colombie-Britannique </region></placeName></affiliation></author><author><name sortKey="Unda, Faride" sort="Unda, Faride" uniqKey="Unda F" first="Faride" last="Unda">Faride Unda</name><affiliation wicri:level="4"><nlm:affiliation>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4</wicri:regionArea><orgName type="university">Université de la Colombie-Britannique</orgName><placeName><settlement type="city">Vancouver</settlement><region type="state">Colombie-Britannique </region></placeName></affiliation></author><author><name sortKey="Mansfield, Shawn D" sort="Mansfield, Shawn D" uniqKey="Mansfield S" first="Shawn D" last="Mansfield">Shawn D. Mansfield</name><affiliation wicri:level="4"><nlm:affiliation>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada shawn.mansfield@ubc.ca.</nlm:affiliation><country wicri:rule="url">Canada</country><wicri:regionArea>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4</wicri:regionArea><orgName type="university">Université de la Colombie-Britannique</orgName><placeName><settlement type="city">Vancouver</settlement><region type="state">Colombie-Britannique </region></placeName></affiliation></author></analytic><series><title level="j">Journal of experimental botany</title><idno type="eISSN">1460-2431</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (enzymology)</term><term>Arabidopsis (growth & development)</term><term>Arabidopsis (metabolism)</term><term>Biomass (MeSH)</term><term>Glucosyltransferases (metabolism)</term><term>Phosphoprotein Phosphatases (metabolism)</term><term>Plants (metabolism)</term><term>Protein Binding (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (croissance et développement)</term><term>Arabidopsis (enzymologie)</term><term>Arabidopsis (métabolisme)</term><term>Biomasse (MeSH)</term><term>Glucosyltransferases (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Phosphoprotein Phosphatases (métabolisme)</term><term>Plantes (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucosyltransferases</term><term>Phosphoprotein Phosphatases</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term><term>Plants</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arabidopsis</term><term>Glucosyltransferases</term><term>Phosphoprotein Phosphatases</term><term>Plantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biomass</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biomasse</term><term>Liaison aux protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Bioinformatic analysis indicates that sucrose phosphate synthase (SPS) contains a putative C-terminal sucrose phosphate phosphatase (SPP)-like domain that may facilitates the binding of SPP. If an SPS-SPP enzyme complex exists, it may provide sucrose biosynthesis with an additional level of regulation, forming a direct metabolic channel for sucrose-6-phosphate between these two enzymes. Herein, the formation of an enzyme complex between SPS and SPP was examined, and the results from yeast two-hybrid experiments suggest that there is indeed an association between these proteins. In addition, in planta bioluminescence resonance energy transfer (BRET) was observed in Arabidopsis seedlings, providing physical evidence for a protein interaction in live cells and in real time. Finally, bimolecular fluorescence complementation (BiFC) was employed in an attempt to detect SPS-SPP interactions visually. The findings clearly demonstrated that SPS interacts with SPP and that this interaction impacts soluble carbohydrate pools and affects carbon partitioning to starch. Moreover, a fusion construct between the two genes promotes plant growth in both transgenic Arabidopsis and hybrid poplar. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25873678</PMID><DateCompleted><Year>2016</Year><Month>04</Month><Day>05</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2431</ISSN><JournalIssue CitedMedium="Internet"><Volume>66</Volume><Issue>14</Issue><PubDate><Year>2015</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Journal of experimental botany</Title><ISOAbbreviation>J Exp Bot</ISOAbbreviation></Journal><ArticleTitle>Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation.</ArticleTitle><Pagination><MedlinePgn>4383-94</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/jxb/erv101</ELocationID><Abstract><AbstractText>Bioinformatic analysis indicates that sucrose phosphate synthase (SPS) contains a putative C-terminal sucrose phosphate phosphatase (SPP)-like domain that may facilitates the binding of SPP. If an SPS-SPP enzyme complex exists, it may provide sucrose biosynthesis with an additional level of regulation, forming a direct metabolic channel for sucrose-6-phosphate between these two enzymes. Herein, the formation of an enzyme complex between SPS and SPP was examined, and the results from yeast two-hybrid experiments suggest that there is indeed an association between these proteins. In addition, in planta bioluminescence resonance energy transfer (BRET) was observed in Arabidopsis seedlings, providing physical evidence for a protein interaction in live cells and in real time. Finally, bimolecular fluorescence complementation (BiFC) was employed in an attempt to detect SPS-SPP interactions visually. The findings clearly demonstrated that SPS interacts with SPP and that this interaction impacts soluble carbohydrate pools and affects carbon partitioning to starch. Moreover, a fusion construct between the two genes promotes plant growth in both transgenic Arabidopsis and hybrid poplar. </AbstractText><CopyrightInformation>© The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maloney</LastName><ForeName>Victoria J</ForeName><Initials>VJ</Initials><AffiliationInfo><Affiliation>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Park</LastName><ForeName>Ji-Young</ForeName><Initials>JY</Initials><AffiliationInfo><Affiliation>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Unda</LastName><ForeName>Faride</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mansfield</LastName><ForeName>Shawn D</ForeName><Initials>SD</Initials><AffiliationInfo><Affiliation>Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada shawn.mansfield@ubc.ca.</Affiliation></AffiliationInfo></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>2015</Year><Month>04</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Exp Bot</MedlineTA><NlmUniqueID>9882906</NlmUniqueID><ISSNLinking>0022-0957</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 2.4.1.-</RegistryNumber><NameOfSubstance UI="D005964">Glucosyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.1.14</RegistryNumber><NameOfSubstance UI="C022698">sucrose-phosphate synthase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.-</RegistryNumber><NameOfSubstance UI="C083874">sucrose-phosphate synthase phosphatase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="D010749">Phosphoprotein Phosphatases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018533" MajorTopicYN="Y">Biomass</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005964" MajorTopicYN="N">Glucosyltransferases</DescriptorName><QualifierName 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Maloney</name></region><name sortKey="Mansfield, Shawn D" sort="Mansfield, Shawn D" uniqKey="Mansfield S" first="Shawn D" last="Mansfield">Shawn D. Mansfield</name><name sortKey="Park, Ji Young" sort="Park, Ji Young" uniqKey="Park J" first="Ji-Young" last="Park">Ji-Young Park</name><name sortKey="Unda, Faride" sort="Unda, Faride" uniqKey="Unda F" first="Faride" last="Unda">Faride Unda</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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