Publikationsserver der Universitätsbibliothek Marburg
Titel:Die Rolle des RNA-bindenden Proteins Rrm4 während des polaren Wachstums von Ustilago maydis
Autor:Koepke, Janine
Weitere Beteiligte: Feldbrügge, Michael (Prof. Dr.)
Veröffentlicht:2011
URI:https://archiv.ub.uni-marburg.de/diss/z2012/0053
DOI: https://doi.org/10.17192/z2012.0053
URN: urn:nbn:de:hebis:04-z2012-00537
DDC: Biowissenschaften, Biologie
Titel (trans.):The role of the RNA-binding protein RRm4 during filamentous growth of Ustilago maydis
Publikationsdatum:2012-02-16
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Sekretion, Ustilago, RNS-Bindungsproteine, Secretion, Proteom-Analyse, mRNA-Transport, RNA-binding protein, Intrazellulärer Transport, mRNA-Transport, 2-D-Gele, Filament

Zusammenfassung:
Polarität und funktionelle Kompartimentierung sind grundlegende Konzepte eukaryontischer Zellen. Der aktive Transport von Vesikeln, Proteinen und mRNA entlang des Zytoskeletts ist ein wichtiger Bestandteil bei der Etablierung und Aufrechterhaltung einer zellulären Polaritätsachse. In Ustilago maydis ist das RNA-bindende Protein Rrm4 am Mikrotubuli-abhängigen mRNA-Transport spezifischer Transkripte während der Filamentbildung beteiligt. Dieser Transportprozess ist wichtig für das polare, filamentöse Wachstum und die Pathogenität des Pilzes. Der Verlust von Rrm4 führt zu erhöhtem bipolarem Wachstum und einer gedrungenen Filamentmorphologie. Die eigentliche zellbiologische Funktion dieses mRNA-Langstreckentransportes ist noch weitestgehend ungeklärt. In dieser Arbeit wurden, basierend auf einer differentiellen Proteom-Analyse zwischen Wildtyp- und rrm4-Filamenten, sieben differentiell exprimierte Proteine identifiziert. Ihre funktionelle Analyse spricht für eine Beteiligung des Rrm4-abhängigen mRNA-Transportes an der Sekretion eines Zellwand-abbauendem Enzyms und der Biogenese von Mitochondrien. Die Deletion von rrm4 resultierte in einer intrazellulären Akkumulation der Endochitinase Cts1, wobei weder die subapikale Lokalisation noch die Aktivität der Cts1 beeinträchtigt wurde. Zudem bestätigte eine FISH-Analyse die cts1-mRNA als direktes Ziel-Transkript von Rrm4 und die Anreicherung der Cts1 konnte auf einen Defekt in der Sekretion von rrm4-Filamente zurückgeführt werden. Des Weiteren wurde anhand von drei differentiell exprimierten Mitochondrienproteinen in rrm4-Filamenten eine Dysfunktion identifiziert, welche sich in einer gesteigerten mitochondriellen Superoxid-Produktion äußerte. Um weitere Einblicke in den mRNA-Transport zu gewinnen, wurde eine Lokalisationsstudie des Poly-(A)-bindende Proteins (Pab1) durchgeführt. In Wildtyp-Filamenten ko-lokalisierte Pab1 mit Rrm4, in vivo, in pendelnden Partikeln. Interessanterweise wurden in rrm4-Filamenten keine sich bewegenden Pab1-Partikel detektiert. Folglich bildet Rrm4 die Haupttransporteinheit des mRNA-Langstreckentransports in Filamenten. Dementsprechend reguliert der Rrm4-abhängige mRNA-Transport apikale Sekretionsprozesse und scheint zusätzlich die gleichmäßige Versorgung des Protein-Imports in die Mitochondrien zu steuern.

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