AgrobacTransV1, Main, Exploration, bibRecord, 000302

Differential Subplastidial Localization and Turnover of Enzymes Involved in Isoprenoid Biosynthesis in Chloroplasts.

Identifieur interne : 000302 ( Main/Exploration ); précédent : 000301; suivant : 000303

Differential Subplastidial Localization and Turnover of Enzymes Involved in Isoprenoid Biosynthesis in Chloroplasts.

Auteurs : Catalina Perello [Espagne] ; Ernesto Llamas [Espagne] ; Vincent Burlat [France] ; Miriam Ortiz-Alcaide [Espagne] ; Michael A. Phillips [Espagne] ; Pablo Pulido [Espagne] ; Manuel Rodriguez-Concepcion [Espagne]

Source :

PloS one [ 1932-6203 ] ; 2016.

RBID : pubmed:26919668

Descripteurs français

English descriptors

KwdEn :
- Agrobacterium tumefaciens (genetics), Aldose-Ketose Isomerases (genetics), Aldose-Ketose Isomerases (metabolism), Arabidopsis (enzymology), Arabidopsis (ultrastructure), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Chloroplasts (enzymology), Chloroplasts (ultrastructure), Genes, Reporter (MeSH), Genetic Vectors (genetics), Plant Leaves (enzymology), Plant Leaves (ultrastructure), Plants, Genetically Modified (MeSH), Protein Aggregates (MeSH), Protein Transport (MeSH), Recombinant Fusion Proteins (metabolism), Subcellular Fractions (enzymology), Terpenes (metabolism), Thylakoid Membrane Proteins (genetics), Thylakoid Membrane Proteins (metabolism), Thylakoids (metabolism), Tobacco (MeSH), Transferases (genetics), Transferases (metabolism).
MESH :
- chemical , genetics : Aldose-Ketose Isomerases, Arabidopsis Proteins, Thylakoid Membrane Proteins, Transferases.
- enzymology : Arabidopsis, Chloroplasts, Plant Leaves, Subcellular Fractions.
- genetics : Agrobacterium tumefaciens, Genetic Vectors.
- chemical , metabolism : Aldose-Ketose Isomerases, Arabidopsis Proteins, Recombinant Fusion Proteins, Terpenes, Thylakoid Membrane Proteins, Thylakoids, Transferases.
- ultrastructure : Arabidopsis, Chloroplasts, Plant Leaves.
- Genes, Reporter, Plants, Genetically Modified, Protein Aggregates, Protein Transport, Tobacco.

Abstract

Plastidial isoprenoids are a diverse group of metabolites with roles in photosynthesis, growth regulation, and interaction with the environment. The methylerythritol 4-phosphate (MEP) pathway produces the metabolic precursors of all types of plastidial isoprenoids. Proteomics studies in Arabidopsis thaliana have shown that all the enzymes of the MEP pathway are localized in the plastid stroma. However, immunoblot analysis of chloroplast subfractions showed that the first two enzymes of the pathway, deoxyxylulose 5-phosphate synthase (DXS) and reductoisomerase (DXR), can also be found in non-stromal fractions. Both transient and stable expression of GFP-tagged DXS and DXR proteins confirmed the presence of the fusion proteins in distinct subplastidial compartments. In particular, DXR-GFP was found to accumulate in relatively large vesicles that could eventually be released from chloroplasts, presumably to be degraded by an autophagy-independent process. Together, we propose that protein-specific mechanisms control the localization and turnover of the first two enzymes of the MEP pathway in Arabidopsis chloroplasts.

DOI: 10.1371/journal.pone.0150539
PubMed: 26919668
PubMed Central: PMC4769067

Affiliations:

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Le document en format XML

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<term>Aldose-Ketose Isomerases (metabolism)</term>
<term>Arabidopsis (enzymology)</term>
<term>Arabidopsis (ultrastructure)</term>
<term>Arabidopsis Proteins (genetics)</term>
<term>Arabidopsis Proteins (metabolism)</term>
<term>Chloroplasts (enzymology)</term>
<term>Chloroplasts (ultrastructure)</term>
<term>Genes, Reporter (MeSH)</term>
<term>Genetic Vectors (genetics)</term>
<term>Plant Leaves (enzymology)</term>
<term>Plant Leaves (ultrastructure)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Protein Aggregates (MeSH)</term>
<term>Protein Transport (MeSH)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Subcellular Fractions (enzymology)</term>
<term>Terpenes (metabolism)</term>
<term>Thylakoid Membrane Proteins (genetics)</term>
<term>Thylakoid Membrane Proteins (metabolism)</term>
<term>Thylakoids (metabolism)</term>
<term>Tobacco (MeSH)</term>
<term>Transferases (genetics)</term>
<term>Transferases (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Agrobacterium tumefaciens (génétique)</term>
<term>Agrégats de protéines (MeSH)</term>
<term>Aldose-ketose isomerases (génétique)</term>
<term>Aldose-ketose isomerases (métabolisme)</term>
<term>Arabidopsis (enzymologie)</term>
<term>Arabidopsis (ultrastructure)</term>
<term>Chloroplastes (enzymologie)</term>
<term>Chloroplastes (ultrastructure)</term>
<term>Feuilles de plante (enzymologie)</term>
<term>Feuilles de plante (ultrastructure)</term>
<term>Fractions subcellulaires (enzymologie)</term>
<term>Gènes rapporteurs (MeSH)</term>
<term>Protéines d'Arabidopsis (génétique)</term>
<term>Protéines d'Arabidopsis (métabolisme)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines de la membrane thylakoïdale (génétique)</term>
<term>Protéines de la membrane thylakoïdale (métabolisme)</term>
<term>Tabac (MeSH)</term>
<term>Terpènes (métabolisme)</term>
<term>Thylacoïdes (métabolisme)</term>
<term>Transferases (génétique)</term>
<term>Transferases (métabolisme)</term>
<term>Transport des protéines (MeSH)</term>
<term>Vecteurs génétiques (génétique)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
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<term>Arabidopsis Proteins</term>
<term>Thylakoid Membrane Proteins</term>
<term>Transferases</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term>
<term>Chloroplastes</term>
<term>Feuilles de plante</term>
<term>Fractions subcellulaires</term>
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<term>Chloroplasts</term>
<term>Plant Leaves</term>
<term>Subcellular Fractions</term>
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<term>Protéines de la membrane thylakoïdale</term>
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<term>Recombinant Fusion Proteins</term>
<term>Terpenes</term>
<term>Thylakoid Membrane Proteins</term>
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<term>Transferases</term>
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<term>Protéines d'Arabidopsis</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de la membrane thylakoïdale</term>
<term>Terpènes</term>
<term>Thylacoïdes</term>
<term>Transferases</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Arabidopsis</term>
<term>Chloroplasts</term>
<term>Plant Leaves</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Genes, Reporter</term>
<term>Plants, Genetically Modified</term>
<term>Protein Aggregates</term>
<term>Protein Transport</term>
<term>Tobacco</term>
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<term>Arabidopsis</term>
<term>Chloroplastes</term>
<term>Feuilles de plante</term>
<term>Gènes rapporteurs</term>
<term>Tabac</term>
<term>Transport des protéines</term>
<term>Végétaux génétiquement modifiés</term>
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<front><div type="abstract" xml:lang="en">Plastidial isoprenoids are a diverse group of metabolites with roles in photosynthesis, growth regulation, and interaction with the environment. The methylerythritol 4-phosphate (MEP) pathway produces the metabolic precursors of all types of plastidial isoprenoids. Proteomics studies in Arabidopsis thaliana have shown that all the enzymes of the MEP pathway are localized in the plastid stroma. However, immunoblot analysis of chloroplast subfractions showed that the first two enzymes of the pathway, deoxyxylulose 5-phosphate synthase (DXS) and reductoisomerase (DXR), can also be found in non-stromal fractions. Both transient and stable expression of GFP-tagged DXS and DXR proteins confirmed the presence of the fusion proteins in distinct subplastidial compartments. In particular, DXR-GFP was found to accumulate in relatively large vesicles that could eventually be released from chloroplasts, presumably to be degraded by an autophagy-independent process. Together, we propose that protein-specific mechanisms control the localization and turnover of the first two enzymes of the MEP pathway in Arabidopsis chloroplasts. </div>
</front>
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<DateCompleted><Year>2016</Year>
<Month>07</Month>
<Day>20</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>02</Month>
<Day>22</Day>
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<Issue>2</Issue>
<PubDate><Year>2016</Year>
</PubDate>
</JournalIssue>
<Title>PloS one</Title>
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</Journal>
<ArticleTitle>Differential Subplastidial Localization and Turnover of Enzymes Involved in Isoprenoid Biosynthesis in Chloroplasts.</ArticleTitle>
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<Abstract><AbstractText>Plastidial isoprenoids are a diverse group of metabolites with roles in photosynthesis, growth regulation, and interaction with the environment. The methylerythritol 4-phosphate (MEP) pathway produces the metabolic precursors of all types of plastidial isoprenoids. Proteomics studies in Arabidopsis thaliana have shown that all the enzymes of the MEP pathway are localized in the plastid stroma. However, immunoblot analysis of chloroplast subfractions showed that the first two enzymes of the pathway, deoxyxylulose 5-phosphate synthase (DXS) and reductoisomerase (DXR), can also be found in non-stromal fractions. Both transient and stable expression of GFP-tagged DXS and DXR proteins confirmed the presence of the fusion proteins in distinct subplastidial compartments. In particular, DXR-GFP was found to accumulate in relatively large vesicles that could eventually be released from chloroplasts, presumably to be degraded by an autophagy-independent process. Together, we propose that protein-specific mechanisms control the localization and turnover of the first two enzymes of the MEP pathway in Arabidopsis chloroplasts. </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Perello</LastName>
<ForeName>Catalina</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Program of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Llamas</LastName>
<ForeName>Ernesto</ForeName>
<Initials>E</Initials>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Burlat</LastName>
<ForeName>Vincent</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>Université de Toulouse, CNRS, UMR 5546, BP 42617 Auzeville, 31326 Castanet-Tolosan, France.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Ortiz-Alcaide</LastName>
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<Initials>M</Initials>
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</AffiliationInfo>
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<ForeName>Michael A</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>Program of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Pulido</LastName>
<ForeName>Pablo</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Program of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.</Affiliation>
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Differential Subplastidial Localization and Turnover of Enzymes Involved in Isoprenoid Biosynthesis in Chloroplasts.

Differential Subplastidial Localization and Turnover of Enzymes Involved in Isoprenoid Biosynthesis in Chloroplasts.

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