Options
Kessler, Félix
Nom
Kessler, Félix
Affiliation principale
Fonction
Professeur ordinaire
Email
felix.kessler@unine.ch
Identifiants
Résultat de la recherche
9 Résultats
Voici les éléments 1 - 9 sur 9
- PublicationMétadonnées seulementIn vivo interaction between atToc33 and atToc159 GTP-binding domains demonstrated in a plant split-ubiquitin system(2009)
; 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 seulementSorting activities in plant cells(2003)
; Eucaryotic cells (plants, animals, fungi, etc.) are subdivided in membrane-bound compartments (organelles), such as the nucleus, mitochondria, chloroplasts, vacuoles, etc. Most organellar proteins are encoded in the nucleus and synthesized in the cytoplasm. Proper sorting of proteins is required to establish and maintain organellar identity. Molecular machineries at the organelle surfaces specifically recognize targeting sequences of their cognate proteins and mediate their translocation across membranes. Proteins destined for the vacuoles are first translocated across the endoplasmic reticulum membrane, packaged into vesicles, transported to the Golgi, where they are sorted into specific vesicles and subsequently carried to the different types of vacuoles. Though plant cells share many features with animal and yeast cells, chloroplasts and distinct lytic and storage vacuoles are unique to plants. Here, we discuss import of proteins into the chloroplast as well as selective sorting of proteins to either the lytic or the storage vacuole. - PublicationMétadonnées seulementAtTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts(2003)
; Schnell, DannyThe translocon of the inner envelope membrane of chloroplasts ( Tic) mediates the late events in the translocation of nucleus-encoded preproteins into chloroplasts. Tic110 is a major integral membrane component of active Tic complexes and has been proposed to function as a docking site for translocation-associated stromal factors and as a component of the protein-conducting channel. To investigate the various proposed functions of Tic110, we have investigated the structure, topology, and activities of a 97.5-kDa fragment of Arabidopsis Tic110 ( atTic110) lacking only the amino-terminal transmembrane segments. The protein was expressed both in Escherichia coli and Arabidopsis as a stable, soluble protein with a high alpha-helical content. Binding studies demonstrate that a region of the at-Tic110-soluble domain selectively associates with chloroplast preproteins at the late stages of membrane translocation. These data support the hypothesis that the bulk of Tic110 extends into the chloroplast stroma and suggest that the domain forms a docking site for preproteins as they emerge from the Tic translocon. - PublicationMétadonnées seulementThe targeting of the atToc159 preprotein receptor to the chloroplast outer membrane is mediated by its GTPase domain and is regulated by GTP(2002)
; Schnell, DannyThe multimeric translocon at the outer envelope membrane of chloroplasts (Toc) initiates the recognition and import of nuclear-encoded preproteins into chloroplasts. Two Toc GTPases, Toc159 and Toc33/34, mediate preprotein recognition and regulate preprotein translocation. Although these two proteins account for the requirement of GTP hydrolysis for import, the functional significance of GTP binding and hydrolysis by either GTPase has not been defined. A recent study indicates that Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, raising the possibility that it might cycle between the cytoplasm and chloroplast as a soluble preprotein receptor. In the present study, we examined the mechanism of targeting and insertion of the Arabidopsis thaliana orthologue of Toc159, atToc159, to chloroplasts. Targeting of atToc159 to the outer envelope membrane is strictly dependent only on guanine nucleotides. Although GTP is not required for initial binding, the productive insertion and assembly of atToc159 into the Toc complex requires its intrinsic GTPase activity. Targeting is mediated by direct binding between the GTPase domain of atToc159 and the homologous GTPase domain of atToc33, the Arabidopsis Toc33/34 orthologue. Our findings demonstrate a role for the coordinate action of the Toc GTPases in assembly of the functional Toc complex at the chloroplast outer envelope membrane. - PublicationMétadonnées seulementA GTPase gate for protein import into chloroplasts(2002)
; Schnell, DannyProtein import into chloroplasts is regulated by the binding and hydrolysis of GTP at two homologous GTPases, Toc34 and Toc159. The crystal structure of the Toc34 GTP-binding domain suggests that GTP-regulated dimerization of the Toc GTPase domains controls the targeting and translocation of preproteins at the chloroplast envelope. - PublicationMétadonnées seulementEssential role of the G-domain in targeting of the protein import receptor atToc159 to the chloroplast outer membrane(2002)
; - PublicationMétadonnées seulementTargeting of an abundant cytosolic form of the protein import receptor at Toc159 to the outer chloroplast membrane(2001)
; - PublicationMétadonnées seulementProtein translocon at the Arabidopsis outer chloroplast membrane(2001)
- PublicationMétadonnées seulementA consensus nomenclature for the protein-import components of the chloroplast envelope(1997)
;