Publikationsserver der Universitätsbibliothek Marburg
Titel:Verbesserte in vitro und in planta DNA-Reparatur durch CPD-Photolyasen.
Autor:Kaiser, Gebhard Alexander
Weitere Beteiligte: Batschauer, Alfred (Prof. Dr.)
Veröffentlicht:2012
URI:https://archiv.ub.uni-marburg.de/diss/z2012/0125
URN: urn:nbn:de:hebis:04-z2012-01255
DOI: https://doi.org/10.17192/z2012.0125
DDC: Biowissenschaften, Biologie
Titel (trans.):Improved in vitro and in planta DNA repair by CPD photolyases.
Publikationsdatum:2012-05-18
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
UV-Toleranz, Thermus thermophilus, Arabidopsis thaliana, Arabidopsis thaliana, Antenna chromophore, Cyclobutane pyrimidine dimmers, Photolyase, Transgene Pflanzen, DNS-Reparatur, Thermus thermophilus, Cyclobutanpyrimidindimer, Photolyase, Antennen-Chromophor, DNA repair

Zusammenfassung:
CPD-Photolyasen sind Enzyme, die lichtabhängig Cyclobutanpyrimidindimer (CPD), eines der Hauptprodukte der UV-abhängigen DNA-Schädigung, reparieren. Sie können bei fast allen Lebewesen gefunden werden und spielen eine zentrale Rolle bei der UV-Resistenz dieser Organismen. Als monomeres, fehlerfrei und energieneutral arbeitendes Reparatursystem sind sie ein geeignetes Werkzeug für die biotechnologische Verbesserung der UV-Toleranz. So könnten sie helfen, den negativen Folgen der erhöhten UV-Belastung, die durch das Ozonloch entstehen, entgegen zu wirken. In Escherichia coli rekombinant überexprimiert bindet die CPD-Photolyase aus Thermus thermophilus FMN als zweiten Kofaktor. Im Gegensatz hierzu binden die meisten anderen diesbezüglich analysierten Photolyasen Methenyltetrahydrofofalt oder Deazaflavin als zweiten Kofaktor. In dieser Arbeit wird durch Absorptions- und Wirkungsspektroskopie gezeigt, dass FMN als Antennenchromophor fungiert und die absorbierte Lichtenergie auf den katalytisch aktiven FAD-Kofaktor überträgt. Hierdurch wird die Photoreduktion und Enzymaktivität der Thermus thermophilus Photolyase deutlich verbessert. Als sessile und photoautotrophe Organismen sind Pflanzen in besonderem Maße UV- und Lichtstress ausgesetzt. Sie besitzen hochkomplexe Signal- und Schutzmechanismen, um sich optimal an die an ihrem Standort vorherrschenden Lichtbedingungen anzupassen. Bei der UV-Toleranz von Pflanzen spielen CPD-Photolyasen eine zentrale Rolle. In dieser Arbeit wurde untersucht, ob die gezielte Verbesserung der Reparatur von CPD-Schäden durch die Überexpression der Arabidopsis CPD-Photolyase in Arabidopsis thaliana einen positiven Effekt auf die UV-Toleranz der Pflanzen hat. Hierfür wurde der kodierende Bereich des CPD- Photolyasegens (At-PHR1) mit dem starken und konstitutiven 35S CaMV Promotor fusioniert und Arabidopsis stabil mit dem resultierenden Konstrukt transformiert. Die stabile Integration des Transgens in das Genom wurde durch Southern Blot überprüft und zudem die Anzahl der T-DNA-Insertionen bestimmt. Die Überexpression wurde dann auf transkriptioneller und posttranskriptioneller Ebene bestimmt. Es konnten deutlich erhöhte Transkript- und Proteinmengen von CPD-Photolyase in den transgenen Linien nachgewiesen werden. Um den Einfluss der At-PHR1-Überexpression auf die Reparatur von CPD-Schäden zu untersuchen, wurden Rosettenblätter mit UV-B und UV-A reichem Licht bestrahlt und die CPD-Akkumulationsrate bestimmt. Hierbei zeigte sich eine deutlich verringerte Akkumulation von CPDs in den transgenen Linien. Weiterhin wurde untersucht, wie sich die Reduktion der CPD-Akkumulation auf das Wachstum der Pflanzen auswirkt. Hierzu wurde das Frischgewicht und der Rosettendurchmesser der unter UV-Stress angezogen Pflanzen bestimmt. Hierbei zeigen die Photolyase-überexprimierenden Pflanzen im Vergleich zum Wildtyp eine deutlich geringere Sensitivität gegenüber UV-B. In der Literatur gibt es widersprüchliche Angaben zur zellulären Lokalisation von CPD-Photolyasen in Pflanzen. Durch Konfokale Laser Scanning Mikroskopie von Arabidopsis Protoplasten, die ein At-PHR1::GFP Fusionsprotein exprimierten, wird hier gezeigt, dass die zelluläre Lokalisation von At-PHR1 auf den Zellkern beschränkt ist.

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