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Kessler, Félix
Résultat de la recherche
Characterization of a Plastoglobule-Localized SOUL4 Heme-Binding Protein in Arabidopsis thaliana
2020-1-31, Kessler, Félix
Heme plays an active role in primary plant metabolic pathways as well as in stress signaling. In this study, we characterized the predicted heme-binding protein SOUL4. Proteomics evidence suggests that SOUL4 is a component of Arabidopsis plastoglobules (PGs, chloroplast lipid droplets). SOUL4 contains heme-binding motifs and the recombinant protein is shown here to bind heme in vitro. Fluorescence-tagged SOUL4 colocalized with the specific PG marker Fibrillin1A (FBN1A) in transiently transformed Nicotiana benthamiana leaves. In addition, SOUL4 cofractionated with another PG marker Fibrillin2 (FBN2) in sucrose gradient ultracentrifugation experiments. In vitro kinase experiments revealed that SOUL4 is phosphorylated by a yet unknown chloroplast protein kinase. Our data demonstrate that SOUL4 is a bona fide PG protein and may function in heme-buffering in the chloroplast.
ABC1K1/PGR6 kinase: a regulatory link between photosynthetic activity and chloroplast metabolism
2014, Martinis, Jacopo, Glauser, Gaëtan, Valimareanu, Sergiu, Stettler, Michaela, Zeeman, Samuel C, Yamamoto, Hiroshi, Shikanai, Toshiharu, Kessler, Félix
Dual targeting of a mature plastoglobulin/fibrillin fusion protein to chloroplast plastoglobules and thylakoids in transplastomic tobacco plants
2013, Shanmugabalaji, Venkatasalam, Besagni, Celine, Eugeni Piller, Lucia, Douet, Véronique, Ruf, Stephanie, Bock, Ralph, Kessler, Félix
Plastid lipid droplets at the crossroads of prenylquinone metabolism
2012, Eugeni Piller, Lucia, Abraham, Marion, Dörmann, Peter, Kessler, Félix, Besagni, Celine
How chloroplasts protect themselves from unfolded proteins
2019-10-15, Kessler, Félix, Longoni, Fiamma
A genetic screen has identified the first signaling component of the unfolded protein response in chloroplasts.
Prenylquinone profiling in whole leaves and chloroplast subfractions
2014, Kessler, Félix, Glauser, Gaëtan
STAY-GREEN and chlorophyll catabolic enzymes interact at light-harvesting complex II for chlorophyll detoxification during leaf senescence in Arabidopsis
2012, Sakuraba, Yasuhito, Schelbert, Silvia, Park, So-Yon, Han, Su-Hyun, Lee, Byoung-Doo, Andrès, Céline Besagni, Kessler, Félix, Hörtensteiner, Stefan, Paek, Nam-Chon
Plastoquinone homoeostasis by Arabidopsis proton gradient regulation 6 is essential for photosynthetic efficiency
2019-6-20, Pralon, Thibaut, Venkatasalam, Shanmugabalaji, Longoni, Fiamma, Ksas, Brigitte, Collombat, Joy, Desmeules, Saskia, Glauser, Gaëtan, Havaux, Michel, Finazzi, Giovanni, Kessler, Félix
Photosynthesis produces organic carbon via a light-driven electron flow from H2O to CO2 that passes through a pool of plastoquinone molecules. These molecules are either present in the photosynthetic thylakoid membranes, participating in photochemistry (photoactive pool), or stored (non-photoactive pool) in thylakoid-attached lipid droplets, the plastoglobules. The photoactive pool acts also as a signal of photosynthetic activity allowing the adaptation to changes in light condition. Here we show that, in Arabidopsis thaliana, proton gradient regulation 6 (PGR6), a predicted atypical kinase located at plastoglobules, is required for plastoquinone homoeostasis, i.e. to maintain the photoactive plastoquinone pool. In a pgr6 mutant, the photoactive pool is depleted and becomes limiting under high light, affecting short-term acclimation and photosynthetic efficiency. In the long term, pgr6 seedlings fail to adapt to high light and develop a conditional variegated leaf phenotype. Therefore, PGR6 activity, by regulating plastoquinone homoeostasis, is required to cope with high light.
A mechanism implicating plastoglobules in thylakoid disassembly during senescence and nitrogen starvation
2013, Besagni, Celine, Kessler, Félix
Fatty acid phytyl ester synthesis in chloroplasts of Arabidopsis
2012, Lippold, Felix, vom Dorp, Katharina, Abraham, Marion, Hölzl, Georg, Wewer, Vera, Yilmaz, Jenny Lindberg, Lager, Ida, Montandon, Cyrille, Besagni, Celine, Kessler, Félix