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The chloroplast import receptor Toc90 partially restores the accumulation of Toc159 client proteins in the Arabidopsis thaliana ppi2 mutant

2011, Infanger, Sibylle, Bischof, Sylvain, Hiltbrunner, Andreas, Agne, Birgit, Baginsky, Sacha, Kessler, Félix

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The acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein

2010, Agne, Birgit, Andres, Charles, Montandon, Cyril, Christ, Bastien, Ertan, Anouk, Jung, Friederike, Infanger, Sibylle, Bischof, Sylvain, Baginsky, Sacha, Kessler, Félix

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In vivo interaction between atToc33 and atToc159 GTP-binding domains demonstrated in a plant split-ubiquitin system

2009, Rahim, Gwendoline, Bischof, Sylvain, Kessler, Félix, Agne, Birgit

The GTPases atToc33 and atToc159 are pre-protein receptor components of the translocon complex at the outer chloroplast membrane in Arabidopsis. Despite their participation in the same complex in vivo, evidence for their interaction is still lacking. Here, a split-ubiquitin system is engineered for use in plants, and the in vivo interaction of the Toc GTPases in Arabidopsis and tobacco protoplasts is shown. Using the same method, the self-interaction of the peroxisomal membrane protein atPex11e is demonstrated. The finding suggests a more general suitability of the split-ubiquitin system as a plant in vivo interaction assay.

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Pheophytin Pheophorbide Hydrolase (Pheophytinase) Is Involved in Chlorophyll Breakdown during Leaf Senescence in Arabidopsis[W],[OA]

2009, Schelbert, Silvia, Aubry, Sylvain, Burla, Bo, Agne, Birgit, Kessler, Félix, Krupinska, Karin, Hörtensteiner, Stefan

During leaf senescence, chlorophyll is removed from thylakoid membranes and converted in a multistep pathway to colorless breakdown products that are stored in vacuoles. Dephytylation, an early step of this pathway, increases water solubility of the breakdown products. It is widely accepted that chlorophyll is converted into pheophorbide via chlorophyllide. However, chlorophyllase, which converts chlorophyll to chlorophyllide, was found not to be essential for dephytylation in Arabidopsis thaliana. Here, we identify pheophytinase (PPH), a chloroplast-located and senescence-induced hydrolase widely distributed in algae and land plants. In vitro, Arabidopsis PPH specifically dephytylates the Mg-free chlorophyll pigment, pheophytin (phein), yielding pheophorbide. An Arabidopsis mutant deficient in PPH (pph-1) is unable to degrade chlorophyll during senescence and therefore exhibits a stay-green phenotype. Furthermore, pph-1 accumulates phein during senescence. Therefore, PPH is an important component of the chlorophyll breakdown machinery of senescent leaves, and we propose that the sequence of early chlorophyll catabolic reactions be revised. Removal of Mg most likely precedes dephytylation, resulting in the following order of early breakdown intermediates: chlorophyll → pheophytin → pheophorbide. Chlorophyllide, the last precursor of chlorophyll biosynthesis, is most likely not an intermediate of breakdown. Thus, chlorophyll anabolic and catabolic reactions are metabolically separated.

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Preparation of multiprotein complexes from Arabidopsis chloroplasts using tandem affinity purification

2011, Andres, Charles, Agne, Birgit, Kessler, Félix

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Nucleotide binding and dimerization at the chloroplast pre?protein import receptor, atToc33, are not essential in vivo but do increase import efficiency

2010, Aronsson, Henrik, Combe, Jonathan, Patel, Ramesh, Agne, Birgit, Martin, Meryll, Kessler, Félix, Jarvis, Paul

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Protein transport in organelles: The Toc complex way of preprotein import

2009, Agne, Birgit, Kessler, Félix

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Modifications at the A-domain of the chloroplast import receptor Toc159

2010, Agne, Birgit, Kessler, Félix

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The TOC complex: preprotein gateway to the chloroplast

2010, Andres, Charles, Agne, Birgit, Kessler, Félix

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Pheophytin pheophorbide hydrolase (pheophytinase) is involved in chlorophyll breakdown during leaf senescence in Arabidopsis

2009, Schelbert, Silvia, Aubry, Sylvain, Burla, Bo, Agne, Birgit, Kessler, Félix, Krupinska, Karin, Hörtensteiner, Stefan