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Kessler, Félix

Nom
Kessler, Félix
Affiliation principale
Fonction
Professeur.e ordinaire
Email
felix.kessler@unine.ch
Identifiants
https://libra.unine.ch/handle/123456789/320
_
0000-0001-6409-5043

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  • Publication
    Métadonnées seulement
    AtTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts
    (2003)
    Inaba, Takehito
    ;
    Li, Ming
    ;
    Alvarez-Huerta, Mayte
    ;
    Kessler, Félix 
    ;
    Schnell, Danny
    The 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.
  • Publication
    Métadonnées seulement
    Protein translocon at the Arabidopsis outer chloroplast membrane
    (2001)
    Hiltbrunner, Andreas
    ;
    Bauer, Jörg
    ;
    Alvarez-Huerta, Mayte
    ;
    Kessler, Félix 
    Chloroplasts are organelles essential for the photoautotrophic growth of plants. Their biogenesis from undifferentiated proplastids is triggered by light and requires the import of hundreds of different precursor proteins from the cytoplasm. Cleavable N-terminal transit sequences target the precursors to the chloroplast where translocon complexes at the outer (Toc complex) and inner (Tic complex) envelope membranes enable their import. In pea, the Toc complex is trimeric consisting of two surface-exposed GTP-binding proteins (Toc159 and Toc34) involved in precursor recognition and Toc75 forming an aequeous protein-conducting channel. Completion of the Arabidopsis genome has revealed an unexpected complexity of predicted components of the Toc complex in this plant model organism: four genes encode homologs of Toc159, two encode homologs of Toc34, but only one encodes a likely functional homolog of Toc75. The availability of the genomic sequence data and powerful molecular genetic techniques in Arabidopsis set the stage to unravel the mechanisms of chloroplast protein import in unprecedented depth.