Publikationsserver der Universitätsbibliothek Marburg
Titel:Funktionelle Analyse des Ustilago maydis Effektorproteins Tin3 im Gencluster 19A
Autor:Neidig, Nina
Weitere Beteiligte: Kahmann, Regine (Prof. Dr.)
Veröffentlicht:2013
URI:https://archiv.ub.uni-marburg.de/diss/z2013/0355
URN: urn:nbn:de:hebis:04-z2013-03553
DOI: https://doi.org/10.17192/z2013.0355
DDC: Biowissenschaften, Biologie
Titel (trans.):Functional analysis of Ustilago maydis effector protein Tin3 in gene cluster 19A
Publikationsdatum:2013-06-26
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Ustilago zeae, Mais, effector, Effektor, autophagy, Proteaseinhibitor, plant pathogen, Autophagie, Pflanzenpathogen

Zusammenfassung:
U. maydis ist ein pilzliches Pflanzenpathogen, das in Mais den sogenannten Maisbeulenbrand auslöst. Die pathogene Entwicklung aller Brandpilze ist an die sexuelle Entwicklung gekoppelt, die durch die Fusion zweier haploider Zellen mit unterschiedlichen Paarungstypen initiiert wird (Bölker et al., 1992). Dies führt zur Bildung eines dikaryotischen Filaments, welches in der Lage ist, Pflanzenzellen mittels spezieller Infektionsstrukturen, den Appressorien, zu penetrieren (Feldbrügge et al., 2004). Während dieses Prozesses wird die Plasmamembran des Wirtes eingestülpt und umhüllt die Pilzhyphen. Dies erzeugt eine spezielle Interaktionszone zwischen Pflanze und Pilz. Biotrophe Pathogene wie U. maydis sind vom Überleben der Wirtspflanze abhängig. Aus diesem Grund ist es essenziell für das Pathogen Erkennung durch das Pflanzenimmunsystem zu vermeiden oder zu unterdrücken, um eine kompatible Interaktion zu etablieren (Doehlemann et al., 2008b). Um diese biotrophe Interaktion mit seiner Wirtspflanze aufzubauen ist U. maydis auf eine Vielzahl von sekretierten Proteinen angewiesen. In dieser Arbeit wurde der U. maydis Effektor Tin3 charakterisiert, der signifikant an der Tumorbildung beteiligt ist und der in Hefe Zwei-Hybrid-Analysen mit einer pflanzlichen Cysteinprotease und dem pflanzlichen Autophagieprotein Beclin1 interagiert (T. Brefort, pers. Mitteilung). Expressionsstudien zeigten, dass tin3 stark und spezifisch während der biotrophen Phase hochreguliert wird. Funktionelle Studien offenbarten eine duale Funktion von Tin3, die über die Interaktion mit zwei Maisproteinen vollzogen wird. Nach der Sekretion in die apoplastische Interaktionszone inhibiert Tin3 sekretierte Mais Cysteinproteasen. In vitro Protease-Aktivitätstests in Kombination mit in vivo Studien zeigen, dass Tin3 in der Lage ist die Cysteinprotease Mir3 und nahe verwandte Proteasen durch Bindung im aktiven Zentrum zu inhibieren. Die biologische Relevanz der roteaseinhibition durch Tin3 zeigte sich in Versuchen, in denen es gelang den Virulenzphänotyp der tin3 Mutante partiell durch Proteaseinhibitoren zu erreichen. Des Weiteren konnte eine zweite Funktion von Tin3 als Autophagie-Repressor postuliert werden, die durch Hefe-Assays und in planta Autophagosomen-Färbungen entdeckt wurde. Die Expression von vier pflanzlichen Autophagiegenen war nach Deletion von tin3 induziert, ein Befund der die Inhibition der Autophagie durch Tin3 unterstützte. H2O2 Akkumulationen in Infektionen mit der tin3 Deletionsmutante deuten an, dass der Tin3 Effektor pflanzliche Abwehrreaktionen durch seine duale Funktion aktiv unterdrückt und deshalb für die Etablierung der Biotrophie benötigt wird.

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