Dokument: Photochemische und strukturelle Untersuchungen neuartiger Bilin-bindender Photorezeptoren
| Titel: | Photochemische und strukturelle Untersuchungen neuartiger Bilin-bindender Photorezeptoren | |||||||
| Weiterer Titel: | Photochemical and structural studies of novel bilin-binding photoreceptors | |||||||
| URL für Lesezeichen: | https://docserv.uni-duesseldorf.de/servlets/DocumentServlet?id=38515 | |||||||
| URN (NBN): | urn:nbn:de:hbz:061-20160615-095816-5 | |||||||
| Kollektion: | Dissertationen | |||||||
| Sprache: | Deutsch | |||||||
| Dokumententyp: | Wissenschaftliche Abschlussarbeiten » Dissertation | |||||||
| Medientyp: | Text | |||||||
| Autor: | M.Sc. Gutt, Alexander [Autor] | |||||||
| Dateien: |
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| Beitragende: | Prof. Dr. Gärtner, Wolfgang [Betreuer/Doktorvater] Prof. Dr. Jaeger, Karl-Erich [Gutachter] | |||||||
| Stichwörter: | Photobiology, Photorezeptoren, GAF-Domänen, Blitzlichtphotolyse | |||||||
| Dewey Dezimal-Klassifikation: | 500 Naturwissenschaften und Mathematik » 540 Chemie | |||||||
| Beschreibungen: | Photorezeptoren sind Licht-detektierende Systeme, die einen äußeren Lichtreiz wahrneh-men und in ein physiologisches Signal umwandeln. Dabei nehmen sie vor allem die Inten-sität, Wellenlänge, Periodizität und Richtung des Lichts wahr. Hier wird besonders die Klasse der Phytochrome bearbeitet. Diese können in fünf wohldefinierte Familien unterteilt werden, welche in erster Linie durch die Struktur der Chromophore und die jeweilige Photochemie bestimmt werden. Eine dieser Familien sind die ‚klassischen‘ Phytochrome, welche wichtige regulatorische Aufgaben in der Photomorphogenese von Pflanzen über-nehmen. Sie zeigen in ihrem photosensorischen Bereich eine PAS-GAF-PHY Struktur und tragen einen offenkettigen Tetrapyrrol- (Bilin) Chromophor, der kovalent an ein Cystein in der GAF-Domäne gebunden ist. In den letzten Jahrzehnten konnten derartige kanonische Phytochrome zusätzlich in Bakterien und Pilzen nachgewiesen werden.
Diese Thesis beinhaltet insbesondere die kinetische Untersuchung verschiedener Photozyklen in Bezug auf mögliche Intermediate und deren Lebenszeiten. Dabei werden klassische Phytochrome aus den Familien der cyanobakteriellen (Cph), der bacteriophy-tochromen (BphP) und der pilzlichen (Fph) Phytochrome als auch die neuartigen Cyanobacteriochrome (CBCRs) untersucht. Die zeitaufgelösten kinetischen Absorptions-messungen wurden mittels der Methode der Blitzlichtphotolyse durchgeführt. i) Vergleich der Photozyklen klassischer Phytochrome Der erste Teil dieser Thesis befasst sich mit der vergleichenden Gegenüberstellung von vier Phytochromen aus drei Phytochrom-Unterfamilien. Untersucht wurde SynCph2(1-2) aus Synechocystis sp. PCC 6803, welches eine GAF-GAF Bidomäne besitzt, wobei ne-ben der Charakterisierung des Wildtyp-Proteins insbesondere die stabilisierende Wirkung der GAF2-Domäne auf den Bilin-Chromophor mit Hilfe von Punktmutationen genauer untersucht wurde. Daneben wurden zwei Bacteriophytochrome, PstBphP1 aus Pseudomo-nas syringae pv. tomato und PaBphP aus Pseudomonas aeruginosa, welches zu den bathy-Phytochromen zählt, sowie ein pilzliches Phytochrom, FphA aus Aspergillus nidulans, spektroskopisch charakterisiert. Es konnte gezeigt werden, dass die Alanin-Mutanten S385A und W389A von SynCph2(1-2) einen deutlichen Einfluss auf den Photozyklus und vor allem auf die Bil-dung des Pfr-Zustandes haben, wohingegen sich der Austausch in eine ähnlich große und aromatische Aminosäure (W389F) nicht auswirkt. Der bathychrome Charakter von PaBphP wirkt sich nicht auf den Photozyklus aus und ist sehr vergleichbar zu den kanoni-schen Phytochromen wie CphA bzw. Cph1, wobei die Konversion aus dem Grundzustand in das Photoprodukt keine sichtbaren Intermediate aufzeigt. PstBphP1 und FphA fehlt im Vergleich zu den kanonischen Phytochromen ein Intermediat beim Übergang in den Pfr-Zustand was auf einen unterschiedlichen Prozess bei der Bildung des Photoprodukts hin-deutet. Die Rückkonversion verläuft bei PstBphP1 ‚klassisch‘, wohingegen bei FphA keine Intermediate identifiziert werden können. ii) Spektroskopische Untersuchung dreier GAF-Domänen der CBCRs Im zweiten Teil der Arbeit werden drei Vertreter der Cyanobacteriochrome unter-sucht. Die CBCRs nehmen in der Klasse der Phytochrome eine außergewöhnliche Stellung ein. Dies zeigt sich u.a. durch ihre Fähigkeit, mit Hilfe einer einzelnen GAF-Domäne den Chromophor kovalent zu binden und einen reversiblen, photochromen Photozyklus zu durchlaufen. Untersucht wurde die GAF3-Domäne von Slr1393 aus Synechocystis sp. PCC 6803, die einen Rot/Grün-Photozyklus zeigt, die GAF1-Domäne aus AphC aus Nostoc sp. PCC 7120, welche einen klassischen Rot/Dunkelrot-Photozyklus aufweist, sowie die GAF3-Domäne aus demselben Organismus mit einem außergewöhnlichen Rot/Orange-Photozyklus, der durch die Erstellung zweier Punktmutationen in der Nähe des Chromo-phors (S487R und S487G) genauer untersucht wurde. Zusätzlich wurde bei 1393gaf3 der Einfluss der Chromophor-Bindung bei Zugabe in vivo als auch in vitro genauer untersucht. Genauere Informationen über Chromophor-Protein Wechselwirkungen konnten durch drei Mutanten (R508N, D531T und N532Y) erhalten werden, die bereits großen Einfluss auf die steady-state Absorption des Pg-Photoproduktes aufweisen. Die CBCR GAF-Domänen zeigen im Vergleich zu den klassischen Phytochromen einen deutlich vereinfachten Photozyklus, der vermutlich auf die geringe Proteingröße und die dadurch mögliche hohe Flexibilität zurückzuführen ist, die es leichter möglich macht, der durch die Chromophor-Isomerisierung erzwungenen Konfirmationsänderungen zu fol-gen. Das außergewöhnliche thermisch sehr instabile und deutlich weniger hypsochrom verschobene Photoprodukt der GAF3-Domäne von AphC lässt sich mit einem möglicher-weise gehinderten Intermediat eines rot/grün Photozyklus erklären. Die generierten Muta-tionen bewirkten eine deutlich stabilisierende Wirkung auf die thermische Rückkehr in den Grundzustand.Photoreceptors are light-detecting systems that convert the external stimulus light into a physiological signal by sensing the intensity, wavelength, periodicity and direction. The focus in this work was set on the phytochrome photoreceptors. Phytochromes can be sepa-rated into five well-defined families, specified for their chromophore structure and their respective photochemistry. One of these families, the ‘classical’ phytochromes, comply important regulatory functions in the photomorphogenesis of plants. Their light-sensing part consists of a PAS-GAF-PHY structure with an open-chain tetrapyrrole (bilin) chromophore covalently bound to a cysteine in the GAF domain. In recent decades canonical phytochromes with such domain architecture could also be detected in bacteria and fungi. This thesis is dedicated in particular to kinetic studies of various photocycles aiming at identification of potential intermediates and their lifetimes. Therefore, classical phy-tochromes from the families of cyanobacterial (Cph), bacteriophytochromes (BphP) and fungal (Fph) phytochromes as well as the novel cyanobacteriochromes (CBCRs) were ex-amined. The time-resolved kinetic absorption measurements were performed using the method of flash photolysis. i) Comparison of the photocycles of classical phytochromes The first part of this thesis deals with the comparative analysis of four phyto-chromes belonging to three phytochrome-subfamilies. The examination of SynCph2(1-2) from Synechocystis sp. PCC 6803, carrying a photosensory GAF-GAF bidomain, is based on the characterization of the wildtype-protein and in particular on the mutational analysis of the stabilizing effect on the chromophore of the GAF2 domain. In addition, two bacteri-ochromes, PstBphP1 from Pseudomonas syringae pv. tomato und PaBphP from Pseudo-monas aeruginosa (member of bathy-phytochromes) as well as a fungal phytochrome, FphA from Aspergillus nidulans, had been spectroscopically characterized. Results reveal an important effect of position 385 and 389 of SynCph2(1-2) on the photocycle. Exchange of these amino acids into alanines (S385A and W389F) affect espe-cially the formation of the Pfr-Photoprodukt, whereas the exchange at position 389 into a similarly large, aromatic amino acid (W389F) has no noticeable effect. The bathochromic nature of PaBphP does not alter the photocycle significantly. Its light-driven conversions are very comparable to those of canonical phytochromes such as CphA or Cph1, although the photoconversion from the parent state to the photoproduct shows no noticeable inter-mediates. Both PstBphP1 and FphA are missing an intermediate in the transition to the Pfr-state (in comparison to canonical phytochromes) suggesting different processes in the for-mation of the photoproduct. The reverse conversion from PstBphP1 proceeds in a ‘classi-cal’ manner, whereas FphA shows no identifiable intermediates. ii) Spectroscopic investigation of three GAF domains from CBCRs In the second part of this work, three representatives of the Cyanobacteriochromes were investigated. The CBCRs assume an exceptional position within the phytochrome photoreceptors. This is apparent, among other things, by their ability to covalently bind the chromophore and undergo a reversible photochromic photocycle with help of only one GAF domain. This study comprised the GAF3 domain from Slr1393 of Synechocystis sp. PCC 6803, showing a red/green photocycle, the GAF1 domain from AphC of Nostoc sp. PCC 7120, showing a classical red/dark red photocycle, as well as the GAF3 domain from the same organism with an exceptional red/orange photocycle. For this CBCR-GAF do-main, also two point mutations located close to the chromophore (S487R and S487G) were included into the time-resolved analysis. The remarkable thermally very unstable and sig-nificantly less hypsochromically shifted photoproduct of the GAF3 domain from AphC can be explained by a possibly hindered intermediate of a red/green photocycle. The generated mutations caused a remarkably stabilizing effect on the thermal recovery to the parent state. In addition, the influence of the chromophore binding mode by either in vivo or in vitro addition was examined in more detail for the 1393gaf3. Further information regarding the chromophore-protein interactions was obtained using three mutants (R508N, D531T and N532Y) who have a major influence on the steady-state absorption of the Pg photo-product. In comparison to the classical phytochromes, the CBCR GAF domains show a sig-nificantly simplified photocycle. This is probably due to the low protein size, maybe ena-bling a high flexibility allowing more easily to follow the forced confirmation changes triggered by the photoisomerization. | |||||||
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| Lizenz: |  Urheberrechtsschutz | |||||||
| Fachbereich / Einrichtung: | Mathematisch- Naturwissenschaftliche Fakultät » WE Chemie » Biochemie | |||||||
| Dokument erstellt am: | 15.06.2016 | |||||||
| Dateien geändert am: | 15.06.2016 | |||||||
| Promotionsantrag am: | 01.04.2016 | |||||||
| Datum der Promotion: | 10.05.2016 |
