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Neuhaus, Jean-Marc

Nom
Neuhaus, Jean-Marc
Affiliation principale
Fonction
Professeur ordinaire
Email
jean-marc.neuhaus@unine.ch
Identifiants
https://libra.unine.ch/handle/123456789/300

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  • Publication
    Accès libre
    The C-terminal tetrapeptide of phaseolin is sufficient to target green fluorescent protein to the vacuole
    (2001)
    Frigerio, Lorenzo
    ;
    Foresti, Ombretta
    ;
    Hernández Felipe, Doramys
    ;
    Neuhaus, Jean-Marc 
    ;
    Vitale, Alessandro
    Phaseolin is a vacuolar storage glycoprotein synthesized as a precursor with a short C-terminal propeptide. We have recently shown that deletion of the last four C-terminal amino acids (AFVY, which are part of, or constitute the propeptide) abolishes vacuolar targeting, causing phaseolin to be secreted. Here we provide biochemical and microscopical evidence that the AFVY tetrapeptide, when fused to a secreted version of green fluorescent protein (GFP), inhibits GFP secretion and leads to its accumulation in vacuoles, where it is processed. This demonstrates that the tetrapeptide contains sufficient information for vacuolar sorting.
  • Publication
    Accès libre
    The Internal Propeptide of the Ricin Precursor Carries a Sequence-Specific Determinant for Vacuolar Sorting
    (2001)
    Frigerio, Lorenzo
    ;
    Jolliffe, Nicholas A.
    ;
    Di Cola, Alessandra
    ;
    Hernández Felipe, Doramys
    ;
    Paris, Nadine
    ;
    Neuhaus, Jean-Marc 
    ;
    Lord, J. Michael
    ;
    Ceriotti, Aldo
    ;
    Roberts, Lynne M.
    Ricin is a heterodimeric toxin that accumulates in the storage vacuoles of castor bean (Ricinus communis) endosperm. Proricin is synthesized as a single polypeptide precursor comprising the catalytic A chain and the Gal-binding B chain joined by a 12-amino acid linker propeptide. Upon arrival in the vacuole, the linker is removed. Here, we replicate these events in transfected tobacco (Nicotiana tabacum) leaf protoplasts. We show that the internal linker propeptide is responsible for vacuolar sorting and is sufficient to redirect the ricin heterodimer to the vacuole when fused to the A or the B chain. This internal peptide can also target two different secretory protein reporters to the vacuole. Moreover, mutation of the isoleucine residue within an NPIR-like motif of the propeptide affects vacuolar sorting in proricin and in the reconstituted A-B heterodimer. This is the first reported example of a sequence-specific vacuolar sorting signal located within an internal propeptide.
  • Publication
    Métadonnées seulement
    The internal propeptide of the ricin precursor carries a sequence-specific determinant for vacuolar sorting
    (2001)
    Frigerio, Lorenzo
    ;
    Jolliffe, Nicholas A
    ;
    Di Cola, Alessandra
    ;
    Hernández Felipe, Doramys
    ;
    Paris, Nadine
    ;
    Neuhaus, Jean-Marc 
    ;
    Lord, J Michael
    ;
    Ceriotti, Aldo
    ;
    Roberts, Lynne M
    Ricin is a heterodimeric toxin that accumulates in the storage vacuoles of castor bean (Ricinus communis) endosperm. Proricin is synthesized as a single polypeptide precursor comprising the catalytic A chain and the Gal-binding B chain joined by a 12-amino acid linker propeptide. Upon arrival in the vacuole, the linker is removed. Here, we replicate these events in transfected tobacco (Nicotiana tabacum) leaf protoplasts. We show that the internal linker propeptide is responsible for vacuolar sorting and is sufficient to redirect the ricin heterodimer to the vacuole when fused to the A or the B chain. This internal peptide can also target two different secretory protein reporters to the vacuole. Moreover, mutation of the isoleucine residue within an NPIR-like motif of the propeptide affects vacuolar sorting in proricin and in the reconstituted A-B heterodimer. This is the first reported example of a sequence-specific vacuolar sorting signal located within an internal propeptide.
  • Publication
    Métadonnées seulement
    The C-terminal tetrapeptide of phaseolin is sufficient to target green fluorescent protein to the vacuole
    (2000)
    Frigerio, Lorenzo
    ;
    Foresti, Ombretta
    ;
    Hernández Felipe, Doramys
    ;
    Neuhaus, Jean-Marc 
    ;
    Vitale, Alessandro
    Phaseolin is a vacuolar storage glycoprotein synthesized as a precursor with a short C-terminal propeptide. We have recently shown that deletion of the last four C-terminal amino acids (AFVY, which are part of, or constitute the propeptide) abolishes vacuolar targeting, causing phaseolin to be secreted. Here we provide biochemical and microscopical evidence that the AFVY tetrapeptide, when fused to a secreted version of green fluorescent protein (GFP), inhibits GFP secretion and leads to its accumulation in vacuoles, where it is processed. This demonstrates that the tetrapeptide contains sufficient information for vacuolar sorting.