Zusammenfassung:
Peroxisomen sind nahezu ubiquitäre, eukaryotische Zellorganellen, die am Abbau von
Fettsäuren und an der Entgiftung des dabei entstehenden Wasserstoffperoxids beteiligt sind.
Neben dieser generellen Funktion beherbergen die Peroxisomen weitere Stoffwechselwege.
Dazu zählen Teile des Glyoxylatwegs in Pflanzen und Pilzen und Stoffwechselwege für die
Bildung von Sekundärmetaboliten. Eine Sonderform der Peroxisomen sind die Glycosomen,
die in Trypanosomen identifiziert werden konnten und einen Großteil der glykolytischen
Enzyme enthalten.
Peroxisomale Matrixproteine enthalten entweder carboxyterminale oder aminoterminale PTS
(„peroxisomal targeting signal“)-Motive (C-terminal: PTS1; N-terminal: PTS2). Diese
werden von zytoplasmatischen Rezeptoren erkannt, die gefaltete und sogar im Komplex
vorliegende Proteine in die Peroxisomen überführen.
In dem pflanzenpathogenen Basidiomyceten Ustilago maydis konnten im Verlauf dieser
Arbeit kryptische PTS1-Motive in einer Reihe von Enzymen aus der Glykolyse bzw.
Gluconeogenese identifiziert werden. Peroxisomale Isoformen dieser Enzyme entstehen durch
alternatives Spleißen oder durch Überlesen von Stopcodons während der Translation. Eine
bioinformatische Analyse ergab, dass in einer Vielzahl von Pilzen Isoformen glykolytischer
Enzyme mit PTS1-Motiv gebildet werden, wobei die Mechanismen zur Herstellung dieser
Isoformen in unterschiedlichen Spezies variieren. Zudem wurden in einigen glykolytischen
Enzymen ungewöhnliche PTS1-Motive gefunden, die vom bisher gültigen Konsensus für
PTS1-Motive abweichen und ebenfalls eine duale Lokalisierung der Enzyme in Peroxisomen
und dem Zytoplasma hervorrufen können.
Bei der genaueren Charakterisierung der Peroxisomen in U. maydis fiel auf, dass diese
Organellen nicht nur für die β-Oxidation von Fettsäuren benötigt werden, sondern auch eine
Funktion beim Zuckerstoffwechsel und der biotrophen Interaktion mit der Wirtspflanze Mais
haben. Außerdem konnte gezeigt werden, dass Peroxisomen in U. maydis an der Synthese
eines extrazellulären Glykolipids beteiligt sind.
Die Ergebnisse dieser Arbeit legen nahe, dass die Peroxisomen in Pilzen durch eine größere
metabolische Vielfalt charakterisiert sind, als bisher angenommen wurde. Die Identifizierung
kryptischer PTS1-Motive in Enzymen aus der Glykolyse lässt die Vermutung zu, dass
Peroxisomen auch in anderen Organismen noch weitere unerwartete Proteine beinhalten.
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