Dokument

Zusammenfassung:
Eisen-Schwefel (Fe-S) Cluster sind wichtige Kofaktoren zahlreicher Proteine und kommen in allen bekannten Lebensformen vor. Fe-S Proteine haben vielfältige Funktionen, u.a. beim Elektronentransport, in Enzymkatalysen und in der Genregulation. In neuester Zeit wurden überdies Fe-S Cluster-haltige Proteine mit einer Funktion in essentiellen zellulären Prozessen wie der DNA-Replikation, DNA-Reparatur, Transkription und Ribosomenassemblierung entdeckt. Die Synthese der Fe-S Cluster und der anschließende Einbau in Apoproteine erfordern in Eukaryoten drei komplexe Synthesemaschinerien, die in den Mitochondrien und im Zytosol lokalisiert sind. Die Reifung zytosolischer und nukleärer Fe-S Proteine wird durch das Zusammenwirken der mitochondrialen Eisen-Schwefel Cluster (ISC)-Assemblierungsmaschinerie, der ISC-Exportmaschinerie und der zytosolischen Eisen-Schwefel Protein Assemblierungs (CIA)-Maschinerie ermöglicht. Die CIA-Maschinerie besteht bisher aus acht Proteinen, jedoch sind deren Interaktionen nicht umfassend beschrieben. Darüber hinaus ist wahrscheinlich, dass weitere CIA-Proteine an diesem komplexen Prozess beteiligt sind. Im ersten Teil dieser Arbeit wurden die Interaktionen der bisher bekannten CIA-Proteine im Modellorganismus Saccharomyces cerevisiae analysiert. Dabei konnte in einer systematischen CIA-Protein Interaktionsanalyse gezeigt werden, dass die einzelnen CIA-Faktoren keinen Superkomplex bilden, sondern in drei funktionelle Subkomplexe unterteilt werden können, die unterschiedlichen Phasen der Biogenese zytosolischer und nukleärer Fe-S Proteine zuzuordnen sind. Auf dem Gerüstproteinkomplex bestehend aus Cfd1-Nbp35 wird in der frühen Phase ein [4Fe-4S] Cluster assembliert. Die für diese Reaktion nötigen Elektronen werden durch den CIA-Subkomplex Dre2-Tah18 bereitgestellt. In der späten Phase der zytosolischen Fe-S Proteinbiogenese wird der neu assemblierte Fe-S Cluster vom Gerüstproteinkomplex auf Apoproteine übertragen. Dieser Schritt erfolgt mithilfe des sog. „CIA-Targetingkomplexes“ bestehend aus Cia1, Cia2 und Met18. Der CIA-Faktor Nar1 nimmt dabei eine intermediäre, noch nicht genau definierte Funktion ein und interagiert sowohl mit den frühen als auch mit den späten Teilen der CIA-Maschinerie. Im zweiten Teil dieser Arbeit wurden die essentiellen Faktoren Yae1 und Lto1 als neue Bestandteile der CIA-Maschinerie entdeckt und charakterisiert. Diese beiden Proteine zeichnen sich durch eine hohe Konservierung aus und bilden einen Komplex, der unter aeroben Bedingungen von besonderer Bedeutung ist. Yae1 und Lto1 wurden durch Auswertung der proteomweiten Interaktionsanalyse als Bindepartner der Komponenten des CIA-Targetingkomplexes identifiziert. Eine frühere systematische Interaktionsstudie hat außerdem gezeigt, dass Yae1 und Lto1 mit dem Fe-S Protein Rli1 interagieren. Die Verbindung zur CIA-Maschinerie war jedoch bis dato nicht bekannt. Es konnte in dieser Arbeit gezeigt werden, dass die Depletion von Yae1 oder Lto1 einen Reifungsdefekt des essentiellen Fe-S Proteins Rli1, nicht aber anderer zytosolischer oder nukleärer Zielproteine zur Folge hat. Darüber hinaus wurde unter Verwendung einer neu etablierten Methode gezeigt, dass Rli1 seine Fe-S Cluster auch nach raschem Abbau von Yae1 stabil gebunden hält, was gegen eine Rolle des Yae1 als Stabilisator der beiden Fe-S Cluster spricht. Diese Befunde legen nahe, dass den beiden Proteinen Yae1 und Lto1 eine Funktion als hoch spezifische Reifungsfaktoren für Rli1 zukommt. Der Komplex aus Yae1 und Lto1 ist in Eukaryoten konserviert und kann durch den humanen YAE1D1-ORAOV1 Komplex funktionell in der Hefe ersetzt werden. Diese Arbeit zeigt, dass bestimmte zytosolische Fe-S Proteine wie Rli1 offensichtlich nicht nur die generelle CIA-Maschinerie, sondern auch die Funktion weiterer spezifischer CIA-Komponenten für die Reifung ihrer Fe-S Cluster benötigen. Eine vergleichbar hohe Substratspezifität wie bei diesen neu entdeckten CIA-Faktoren wurde kürzlich auch für den humanen CIA-Faktor CIA2A beschrieben, der ausschließlich für die Maturierung des zytosolischen Fe-S Proteins IRP1 verantwortlich ist. Zukünftige Untersuchungen müssen deshalb die interessante Frage angehen, ob nicht weitere CIA-Faktoren existieren, die auf bisher unbekannte Weise die Reifung eukaryotischer Fe-S Proteine unterstützen. Ein weiteres Ziel wird die Klärung der Frage sein, nach welchem molekularen Mechanismus solch hoch spezifische Faktoren den Fe-S Cluster-Einbau in Zielproteine gewährleisten.

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