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Kessler, Félix
Nom
Kessler, Félix
Affiliation principale
Fonction
Professeur.e ordinaire
Email
felix.kessler@unine.ch
Identifiants
Résultat de la recherche
Voici les éléments 1 - 10 sur 21
- PublicationMétadonnées seulementThe 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 - PublicationMétadonnées seulement
- PublicationMétadonnées seulementModifications at the A-domain of the chloroplast import receptor Toc159(2010)
;Agne, Birgit - PublicationMétadonnées seulementThe acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein(2010)
;Agne, Birgit; ;Montandon, Cyril ;Christ, Bastien ;Ertan, Anouk ;Jung, Friederike ;Infanger, Sibylle ;Bischof, Sylvain ;Baginsky, Sacha - PublicationMétadonnées seulementNucleotide 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; Jarvis, Paul - PublicationMétadonnées seulementThe TOC complex: preprotein gateway to the chloroplast(2010)
; ;Agne, Birgit - PublicationAccès libreA Toc159 Import Receptor Mutant, Defective in Hydrolysis of GTP, Supports Preprotein Import into Chloroplasts(2009)
;Agne, Birgit ;Infanger, Sibylle ;Wang, Fei ;Hofstetter, Valère ;Rahim, Gwendoline ;Martin, Meryll ;Lee, Dong Wook ;Hwang, Inhwan ;Schnell, DannyThe heterotrimeric Toc core complex of the chloroplast protein import apparatus contains two GTPases, Toc159 and Toc34, together with the protein-conducting channel Toc75. Toc159 and Toc34 are exposed at the chloroplast surface and function in preprotein recognition. Together, they have been shown to facilitate the import of photosynthetic proteins into chloroplasts in Arabidopsis. Consequently, the ppi2 mutant lacking at Toc159 has a non-photosynthetic albino phenotype. Previous mutations in the conserved G1 and G3 GTPase motifs abolished the function of Toc159 in vivo by disrupting targeting of the receptor to chloroplasts. Here, we demonstrate that a mutant in a conserved G1 lysine (atToc159 K868R) defective in GTP binding and hydrolysis can target and assemble into Toc complexes. We show that atToc159 K868R can support protein import into isolated chloroplasts, albeit at lower preprotein binding and import efficiencies compared with the wild-type receptor. Considering the absence of measurable GTPase activity in the K868R mutant, we conclude that GTP hydrolysis at atToc159 is not strictly required for preprotein translocation. The data also indicate that preprotein import requires at least one additional GTPase other than Toc159. - PublicationMétadonnées seulementIn vivo interaction between atToc33 and atToc159 GTP-binding domains demonstrated in a plant split-ubiquitin system(2009)
;Rahim, Gwendoline ;Bischof, Sylvain; Agne, BirgitThe 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. - PublicationMétadonnées seulementProtein transport in organelles: The Toc complex way of preprotein import(2009)
;Agne, Birgit - PublicationMétadonnées seulementPheophytin pheophorbide hydrolase (pheophytinase) is involved in chlorophyll breakdown during leaf senescence in Arabidopsis(2009)
;Schelbert, Silvia ;Aubry, Sylvain ;Burla, Bo ;Agne, Birgit; ;Krupinska, KarinHörtensteiner, Stefan
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