Publikationsserver der Universitätsbibliothek Marburg
Titel:Import peroxisomaler Matrixproteine über die Ustilago maydis Rezeptoren Pex5a, Pex5b und Pex7
Autor:Ast, Julia
Weitere Beteiligte: Bölker, Michael (Prof. Dr.)
Veröffentlicht:2017
URI:https://archiv.ub.uni-marburg.de/diss/z2017/0080
DOI: https://doi.org/10.17192/z2017.0080
URN: urn:nbn:de:hebis:04-z2017-00808
DDC: Biowissenschaften, Biologie
Titel (trans.):Import of peroxisomal matrix proteins by the receptors Pex5a, Pex5b and Pex7 of Ustilago maydis
Publikationsdatum:2017-09-14
Lizenz:https://creativecommons.org/licenses/by/4.0

Dokument

Schlagwörter:
PTS2, Ustilago, Pex7, import, PTS1, peroxisome, Pex5, Peroxisom, Import, Pex5, Ustilago maydis, Pex7, Ustilago maydis

Zusammenfassung:
Peroxisomen sind von einer einfachen Membran umschlossene Organellen, die in den meisten eukaryotischen Zellen vorkommen. Sie sind essentiell für den Abbau von Fettsäuren und entgiften das dabei entstehende Wasserstoffperoxid. Peroxisomen und ihr enzymatischer Inhalt passen sich an die Umgebungsbedingungen und den Lebenszyklus an. Dabei können sich diese Organellen sogar so weit spezialisieren, dass sie neue Funktionen übernehmen. Trotz ihrer Diversität ist das Importsystem, mit dem lösliche Proteine aus dem Zytosol in die Peroxisomen transportiert werden, hoch konserviert. Peroxisomale Matrixproteine werden im Zytosol translatiert und im gefalteten Zustand von einem löslichen Rezeptor in die Peroxisomen importiert. Die Erkennung erfolgt dabei über peroxisomale Targeting-Signale (PTS). Diese Signale befinden sich entweder nahe des N-terminalen Endes (PTS2) oder am C-terminalen Ende (PTS1) des Proteins und werden von dem PTS2-Rezeptor Pex7 oder dem PTS1-Rezeptor Pex5 gebunden. Im Folgenden wird das geladene Matrixprotein, das Cargo, zur peroxisomalen Membran gebracht und in die Matrix transloziert. Abschließend werden die Rezeptoren recycelt und stehen für eine neue Importrunde zur Verfügung. Der phytopathogene Basidiomycet Ustilago maydis weist zwei Pex5 und ein Pex7 auf. Der Phänotyp einer pex5b-Deletionsmutante ist prominenter als der einer pex5a-Deletion. Beide Mutanten zeigen eine reduzierte Filamentbildung, verminderte Virulenz und ein eingeschränktes Wachstum auf Fettsäuren. Im Verlauf dieser Arbeit konnte nachgewiesen werden, dass sowohl Pex5a als auch Pex5b essentiell für die Verstoffwechselung von Fettsäuren sind, während der PTS2-Rezeptor unter diesen Bedingungen nicht benötigt wird. In einer bioinformatischen Analyse konnten PTS2-Proteine identifiziert werden, wobei von vielen keine Funktion bekannt ist und einige zusätzliche Zielsteuerungssignale aufweisen. Der überwiegende Teil der peroxisomalen Matrixenzyme erreicht dieses Organell über die PTS1-Rezeptoren. Bei Lokalisationsuntersuchungen von PTS1-Proteinen fiel auf, dass diese immer im Zytosol verbleiben, wenn pex5b deletiert war. Auf einige traf das auch nach Deletion von pex5a zu, obwohl diese Proteine in Wildtyp-Zellen peroxisomale Lokalisierung zeigten. Folglich werden für den Import mancher PTS1-Proteine sowohl Pex5a als auch Pex5b benötigt. Weiterhin konnte gezeigt werden, dass Pex5a nur in Anwesenheit von Pex5b den Importzyklus durchlaufen kann und dass diese Abhängigkeit über die N-terminale Domäne (NTD) von Pex5b vermittelt wird. Die NTD von Pex5b enthält auch die Pex7-bindende Domäne und ist für den Pex7-vermittelten PTS2-Import essentiell. Zudem konnte gezeigt werden, dass die Cargo-Pex5-Interaktion nicht ausschließlich über die PTS1-Bindetasche von Pex5 vermittelt wird und so zusätzlich zwischen Cargos diskrimiert werden könnte. Da pex5a und pex5b außerdem während des Lebenszyklus von U. maydis differentiell exprimiert werden, legt dies nahe, dass Pex5a und Pex5b als Regulatoren des peroxisomalen Proteoms fungieren. Dabei könnten sie das enzymatische Repertoire der Peroxisomen an den durch die Umgebungsbedingungen bestimmten Bedarf anpassen.

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