The discovery of SycO highlights a new function for type III secretion effector chaperones

Michel Letzelter, Isabel Sorg, Luís Jaime Mota, Salome Meyer, Jacqueline Stalder, Mario Feldman, Marina Kuhn, Isabelle Callebaut, Guy R Cornelis

    Résultats de recherche: Contribution à un journal/une revueArticleRevue par des pairs

    Résumé

    Bacterial injectisomes deliver effector proteins straight into the cytosol of eukaryotic cells (type III secretion, T3S). Many effectors are associated with a specific chaperone that remains inside the bacterium when the effector is delivered. The structure of such chaperones and the way they interact with their substrate is well characterized but their main function remains elusive. Here, we describe and characterize SycO, a new chaperone for the Yersinia effector kinase YopO. The chaperone-binding domain (CBD) within YopO coincides with the membrane localization domain (MLD) targeting YopO to the host cell membrane. The CBD/MLD causes intrabacterial YopO insolubility and the binding of SycO prevents this insolubility but not folding and activity of the kinase. Similarly, SycE masks the MLD of YopE and SycT covers an aggregation-prone domain of YopT, presumably corresponding to its MLD. Thus, SycO, SycE and most likely SycT mask, inside the bacterium, a domain needed for proper localization of their cognate effector in the host cell. We propose that covering an MLD might be an essential function of T3S effector chaperones.
    langue originaleAnglais
    Pages (de - à)3223-33
    Nombre de pages11
    journalThe EMBO journal
    Volume25
    Numéro de publication13
    Les DOIs
    Etat de la publicationPublié - 2006

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