Publikationsserver der Universitätsbibliothek Marburg
Titel:Vergleichende Analysen der nukleär/zytoplasmatischen Exporteigenschaften von SR-ähnlichen Proteinen und ihre regulatorische Funktion im mRNA Spleißing-Prozess
Autor:Hackmann, Alexandra
Weitere Beteiligte: Krebber, Heike (Prof.)
Veröffentlicht:2010
URI:https://archiv.ub.uni-marburg.de/diss/z2011/0456
DOI: https://doi.org/10.17192/z2011.0456
URN: urn:nbn:de:hebis:04-z2011-04561
DDC: Biowissenschaften, Biologie
Titel (trans.):Comparative analysis of the nuclear/cytoplasmic export requirements of SR-like proteins and their regulatory function in mRNA splicing process
Publikationsdatum:2012-02-16
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Intracellular transport, Gbp2, messenger-RNP, RNS-Spleißen, Npl3, Messenger-RNP, Kernporen-Komplex, Gbp2, Npl3, Saccharomyces cerevisiae, Intrazellulärer Transport, Messenger-RNP, Saccharomyces cerevisiae, Saccharomyces cerevisiae

Zusammenfassung:
Eukaryontische Zellen zeichnen sich durch ihre Kompartimentierung in Zytoplasma und Zellkern aus, die eine regulierte Genexpression ermöglicht. Im Zellkern erfolgt die Transkription der Gene in prä-mRNAs, die nach extensiver Prozessierung zur Export kompetenten mRNA im Ribonukleoprotein-Komplex („messenger ribonucleoprotein particle“ = mRNP) heranreifen. Die SR-ähnlichen mRNA Bindeproteine Npl3p, Gbp2p und Hrb1p assoziieren während der Transkription mit der mRNA im Zellkern und Npl3p interagiert mit dem Export Rezeptor Mex67p-Mtr2p, der die Export-kompetente mRNA durch die Kernporen-Komplexe der Kernmembran in das Zytoplasma transportiert. Dort erfolgt an den Ribosomen die Proteintranslation anhand der mRNA kodierten genetischen Information. Npl3p ist in vielen Saccharomyces cerevisiae Stämmen ein essentielles Protein und Mutationen führen zu mRNA Export-Defekten. In einem weltweiten Deletionsprojekt wurde eine überlebensfähige NPL3-Deletion im Stammhintergund BY4741 hergestellt. Interessanterweise sind in npl3∆ keine signifikanten mRNA Export Defekte vorhanden, was auf eine weitere, bisher unbekannte Funktion von NPL3 hindeutet. In Lokalisationsstudien wurden jedoch nukleäre Export-Defekte der ribosomalen prä-60S, nicht aber der 40S Untereinheit in npl3∆-Zellen nachgewiesen. Npl3p interagiert physikalisch sowohl über das ribosomale Protein Rpl25p als auch über die 25S rRNA mit der prä-60S Untereinheit. Eine Funktion von Npl3p in der Prozessierung des ribosomalen Vorläufers ist aufgrund von nicht detektierten rRNA Prozessierungsdefekten und nukleolaren Mislokalisationen in npl3∆ unwahrscheinlich. Npl3p interagiert mit den Faktoren der Export kompetenten prä-60S Untereinheit Nmd3p und dem ebenfalls im prä-60S Export agierenden Export-Rezeptor Mex67p. Eine Deletion von NPL3 beeinflußt jedoch nicht die Rekrutierung dieser prä-60S Exportfaktoren zur ribosomalen Untereinheit. Da Npl3p die prä-60S Untereinheit physikalisch bindet und seine Deletion nukleäre Export-Defekte hervorruft, wirkt Npl3p als unabhängiger Exportadapter im prä-60S Transportprozess. Npl3p hat das Potential den Kontakt zwischen der prä-60S Untereinheit und den Kernporen-Komplexen über eine physikalische Interaktion mit dem Nup60p assoziierten Mlp1p zu vermitteln. In einem zweiten Kapitel dieser Arbeit erfolgte die vergleichende Analyse der Exporteigenschaften von Gbp2p, Hrb1p und Npl3, welche erstmalig eine Verbindung zum Spleißing-Prozess aufzeigt. In einem „Screen“ wurden die Spleißingfaktor-Mutanten prp8-908/988 und prp17-Q336* identifiziert, die starke nukleäre Export-Defekte von Gbp2p und Hrb1, nicht aber von Npl3p hervorrufen. GBP2 und HRB1 Deletionen interagieren genetisch mit diesen Spleißingfaktor-Mutanten der Spleißing Spätphase, während eine NPL3 Deletion weder genetisch noch physikalisch mit diesen Faktoren interagiert. Gbp2p und Hrb1p zeigen Protein-Protein Wechselwirkungen mit Prp17p und mit Prp43p des postspleißosomalen Komplexes. Die nukleären Mislokalisationen von Gbp2p und Hrb1p in Spleißing-faktor Mutanten der Spleißing Spätphase beruhen auf eine starke Störung der mRNA Bindung, die in RNA-Co IP Studien ermittelt wurden. Für Gbp2p und Hrb1p wurde in RIP-Chip und qRT-PCR-Studien eine präferentielle Bindung für mRNAs identifiziert, die Intronsequenzen enthalten. Marginale Spleißing Defekte, aber signifikante Proteinexpressionsabnahmen Intron-haltiger Gene wurden vor allem in der Doppel-Deletion gbp2∆ hrb1∆ nachgewiesen. Gbp2p und Hrb1p interagieren mit dem Export-Rezeptor Mex67p und sind somit als neue mRNA Export Adapter identifiziert worden. In Spleißingfaktor-Mutanten sind diese Adapter-Rezeptor Bindungen gestört, wodurch der Export von ungespleißten mRNAs vermutlich zurückgehalten wird. Gbp2p und Hrb1p zeigen eine Verbindung zum Kernporen-Komplex assoziierten Mlp1p. Dieser Faktor hat eine Funktion in der finalen Qualitätskontrolle von gespleißten mRNAs bevor diese den Zellkern verlassen können. Daraus ergibt sich folgendes Modell: Gbp2p und Hrb1p werden Spleißing-abhängig zur mRNA rekrutiert und unterstützen den Export von gespleißten mRNAs über eine Interaktion mit dem Export-Rezeptor Mex67p. Im Gegensatz dazu agiert Npl3p als universeller Export-Adapter, der unabhängig vom Intron-Status der mRNA Mex67p bindet. Bekannterweise wird Npl3p über die RNA Polymerase II frühzeitig auf alle mRNAs geladen, während Gbp2p und Hrb1p in der Elongations- phase zur mRNA gelangen. Eine stabile Assoziation von Gbp2p und Hrb1p mit der mRNA erfolgt erst durch die Assemblierung des Spleißosom, mit dessen Komponenten der Spleißing-Spätphase sie physikalisch interagieren. Diese Wechselwirkungen unterstützen Spleißing und ermöglichen über die sich anschließende Adapter-Rezeptor Interaktion einen effizienten und kontrollierten Export von gespleißten mRNAs.

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