Molecular Analysis and Localization of CaARA7 a Conventional RAB5 GTPase from Characean Algae

Titel in Übersetzung: Molecular analysis and localization of CaARA7 a conventional RAB5 GTPase from characean algae

Marion C Hoepflinger, Anja Geretschlaeger, Aniela Sommer, Margit Hoeftberger, Christina Hametner, Takashi Ueda, Ilse Foissner

    Publikation: Beitrag in FachzeitschriftArtikel

    Abstract

    RAB5 GTPases are important regulators of endosomal membrane traffic. Among them Arabidopsis thaliana ARA7/RABF2b is highly conserved and homologues are present in fungal, animal and plant kingdoms. In land plants ARA7 and its homologues are involved in endocytosis and transport towards the vacuole. Here we report on the isolation of an ARA7 homologue (CaARA7/CaRABF2) in the highly evolved characean green alga Chara australis. It encodes a polypeptide of 202 amino acids with a calculated molecular mass of 22.2 kDa and intrinsic GTPase activity. Immunolabelling of internodal cells with a specific antibody reveals CaARA7 epitopes at multivesicular endosomes (MVEs) and at MVE-containing wortmannin (WM) compartments. When transiently expressed in epidermal cells of Nicotiana benthamiana leaves, fluorescently tagged CaARA7 localizes to small organelles (putative MVEs) and WM compartments, and partially colocalizes with AtARA7 and CaARA6, a plant specific RABF1 GTPase. Mutations in membrane anchoring and GTP binding sites alter localization of CaARA7 and affect GTPase activity, respectively. This first detailed study of a conventional RAB5 GTPase in green algae demonstrates that CaARA7 is similar to RAB5 GTPases from land plants and other organisms and shows conserved structure and localization.

    OriginalspracheEnglisch
    Seiten (von - bis)534-554
    Seitenumfang21
    FachzeitschriftTraffic
    Jahrgang16
    Ausgabenummer5
    DOIs
    PublikationsstatusVeröffentlicht - Mai 2015

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    © 2015 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.

    Systematik der Wissenschaftszweige 2012

    • 106 Biologie

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