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Kessler, Félix
Nom
Kessler, Félix
Affiliation principale
Fonction
Professeur.e ordinaire
Email
felix.kessler@unine.ch
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4 Résultats
Voici les éléments 1 - 4 sur 4
- 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 seulementPlastid proteome assembly without Toc159: photosynthetic protein import and accumulation of N-acetylated plastid precursor proteins(2011)
;Bischof, Sylvain ;Baerenfaller, Katja ;Wildhaber, Thomas ;Troesch, Raphael ;Vidi, Pierre-Alexandre ;Roschitzki, Bernd ;Hirsch-Hoffmann, Matthias ;Hennig, Lars; Gruissem, Wilhelm - 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 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.