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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
    Interaction of the protein import and folding machineries in the chloroplast
    (1996)
    Kessler, Félix 
    ;
    Blobel, Gunter
    We report the molecular cloning of import intermediate associated protein (IAP) 100, a 100-kDa protein of the chloroplast protein import machinery of peas, IAP100 contains two potential alpha-helical transmembrane segments and also behaves like an integral membrane protein, It was localized to the inner chloroplast envelope membrane, Immunoprecipitation experiments using monospecific anti-IAP100 antibodies and a nonionic detergent-generated chloroplast lysate gave the following results, (i) The four integral membrane proteins of the outer chloroplast import machinery were not coprecipitated with IAP100 indicating that the inner and outer membrane import machineries are not coupled in isolated chloroplasts. (ii) the major protein that coprecipitated with IAP100 was identified as stromal chaperonin 60 (cpn60); the association of IAP100 and cpn60 was specific and was abolished when immunoprecipitation vias carried out in the presence of ATP, (iii) In a lysate from chloroplasts that had been preincubated for various lengths of time in an import reaction with radiolabeled precursor (pS) of the small subunit of Rubisco, we detected coimmunoprecipitation of IAP100, cpn60, and the imported mature form (S) of precursor, Relative to the time course of import, coprecipitation of S first increased and then decreased, consistent with a transient association of the newly imported S with the chaperonin bound to IAP100. These data suggest that IAP100 serves in recruiting chaperonin for folding of newly imported proteins.
  • Publication
    Métadonnées seulement
    Isolation of components of the chloroplast protein import machinery
    (1994)
    Schnell, Danny
    ;
    Kessler, Félix 
    ;
    Blobel, Gunter
    Components of the protein import machinery of the chloroplast were isolated by a procedure in which the import machinery was engaged in vitro with a tagged import substrate under conditions that yielded largely chloroplast envelope-bound import intermediates. Subsequent detergent solubilization of envelope membranes showed that six envelope polypeptides copurified specifically and, apparently, stoichiometrically with the import intermediates. Four of these polypeptides are components of the outer membrane import machinery and are associated with early import intermediates. Two of these polypeptides have been characterized. One is a homolog of the heat shock protein hsp70; the other one is a channel-protein candidate.