Dokument

Summary:
Phytochrome sind Bilin-bindende Photorezeptoren, die zwischen einer Rotlicht- (Pr) und einer Dunkelrotlicht-absorbierenden Form (Pfr) photokonvertieren können. SynCph2 aus Synechocystis sp. PCC 6803 weist einen GAF1-GAF2-GGDEF1*-EAL-GAF3-GGDEF2 Domänenaufbau auf, was darauf hindeutet, dass es sich um ein Hybrid aus einem GAF-GAF-Bidomänen-Phytochrom und einem Cyanobakteriochrom (GAF3) handelt. Diese Arbeit enthält eine detaillierte Analyse des N-terminalen GAF1-GAF2 Moduls. SynCph2(1-2) weist eine rot/dunkelrote Photochemie auf; somit ist die GAF2 Domäne in der Lage, die kanonische PHY Domäne zu ersetzen. Der Chromophor PCB ist kovalent an Cys-129 in der GAF1 Domäne gebunden. In Kooperation mit der Gruppe von P. Hildebrandt konnten wir zeigen, dass alle vier Pyrrolstickstoffe sowohl in Pr (ZZZssa) als auch in Pfr (ZZEssa) protoniert sind. In der Fern-UV CD Spektroskopie konnte ein 3%iger Anstieg des α-Helix Gehaltes in der Pr → Pfr Phototransformation festgestellt werden. Desweiteren erhöht sich in Pfr der hydrodynamische Durchmesser von SynCph2(1-2). Die Kristallstruktur von SynCph2(1-2) in der Pr Konformation konnte bei einer Auflösung von 2,6 Å gelöst werden. Das Protein kristallisiert als antiparalleles Dimer, wobei die GAF1 und GAF2 Domänen durch einen α-helikalen Linker verbunden sind. Die GAF2 Domäne ahmt den strukturellen Aufbau der kanonischen PHY Domäne nach, indem sie mit einem Zungen-ähnlichen Vorsprung die Chromophorbindungstasche in GAF2 abdeckt. Der Chromophor PCB in seiner ZZZssa Konformation ist nicht planar, sondern zeigt eine Verkippung der B-/C- sowie der C-/D-Ringe gegeneinander. Basierend auf der Kristallstruktur führten wir eine Mutagenesestudie durch, die die D-Ringumgebung und Propionatinteraktionen des Chromophors sowie die Zungenregion umfasste. Dabei unterscheiden sich die B-Ringpropionatinteraktionen von kanonischen Phytochromen und scheinen vom Typ der Effektordomäne abzuhängen. Die Analyse konservierter Motive in der Zungenregion führte zu einem Modell, das die strukturellen Änderungen während der Photokonversion beschreibt. Dabei wird die Zungenregion durch einen Trp-Positionstausch in den W(G/A)G und WxE Motiven verdreht, die als Anker die Pfr Struktur stabilisieren. Desweiteren bricht die Asp-Arg Salzbrücke, das PRxSF Motiv wird reorientiert und wahrscheinlich α-helikal, wodurch sich die neue Asp-Ser Interaktion ausbilden kann. Eine nähere Untersuchung des Photozyklus’ von SynCph2(1-2) ergab vier Intermediate in der Pr → Pfr und drei in der Pfr → Pr Photokonversion. Trotz ihrer Distanz von ~13 Å und ~15 Å zum D-Ring des Chromophors, beeinflussen Ser-385 aus dem PRxSF und Trp-389 aus dem WxE Motiv die Bildung des Pfr Zustandes. Die S385A Mutation wirkt sich auf das letzte Intermediat der Pr → Pfr Photokonversion und das erste der Rückreaktion aus. Die W389A Mutation beeinflusst schon das dritte Intermediat, das direkt in einen degenerierten Rotlicht-adaptierten Zustand zerfällt. Die drei PDeg → Pr Intermediate unterscheiden sich alle von SynCph2(1-2). Ein Austausch von Trp-389 mit Phenylalanin stellt das Wildtyp-ähnliche Verhalten wieder her. Wir schlussfolgern, dass in den ersten zwei Intermediaten nur der Chromophor und seine nächste Umgebung von Veränderungen betroffen sind. Während der Bildung von Intermediat R2 treten die strukturellen Änderungen in der Zungenregion auf, die den oben postulierten Tryptophanwechsel beinhalten. Die Bildung des letzten Intermediates leitet die Reorientierung von Ser-385 und die Ausbildung des Wasserstoffbrückennetzwerkes ein, das das Aspartat der GAF1 Domäne sowie Ser-385 einschließt. Im Rahmen einer Arbeit, die mit P. Savakis, S. De Causmaecker und V. Angerer in Kooperation mit der Gruppe von A. Wilde ausgeführt wurde, konnten wir die Rolle des C-terminalen GAF3-GGDEF2 Moduls beleuchten. SynCph2(5-6) photokonvertiert zwischen einer Blau- (Pb) und Grünlicht-absorbierenden (Pg) Form. PCB ist kovalent an Cys-1022 und Cys-994 gebunden und wird zu PVB autoisomerisiert. Das Modul ist in der Lage, lichtabhängig c-di-GMP in der GGDEF2 Domäne herzustellen, wobei der Signalzustand Pg auch in in vivo Studien in Synechocystis sp. bestätigt wurde. Unter Blaulichtbedingungen führt die c-di-GMP Herstellung von SynCph2(5-6) zu einer Inhibierung der Phototaxis. Durch Koproduktion von SynCph2(5-6) und SynCph2(1-4) konnte der Wildtypphenotyp unter Weisslicht wiederhergestellt werden, was zeigt, dass SynCph2(1-4) eine enzymatische Aktivität aufweist, die durch die c-di-GMP-abbauende EAL Domäne verursacht wird. Die hier dargelegten Studien von SynCph2 zeigen das Zusammenspiel von photochemischen und strukturellen Eigenschaften in den Pr / Pfr und Pb / Pg interkonvertierenden Modulen sowie ihre Bedeutung in vivo. Zukünftige Studien profitieren von den Einblicken in die Signaltransduktion in Phytochromen und insbesondere von der Trp-Schalterhypothese.

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