Dokument: Biochemische Charakterisierung von modularen dirigierenden Proteinen
| Titel: | Biochemische Charakterisierung von modularen dirigierenden Proteinen | |||||||
| URL für Lesezeichen: | https://docserv.uni-duesseldorf.de/servlets/DocumentServlet?id=65097 | |||||||
| URN (NBN): | urn:nbn:de:hbz:061-20240312-112646-7 | |||||||
| Kollektion: | Dissertationen | |||||||
| Sprache: | Deutsch | |||||||
| Dokumententyp: | Wissenschaftliche Abschlussarbeiten » Dissertation | |||||||
| Medientyp: | Text | |||||||
| Autor: | Huwa, Nikolai [Autor] | |||||||
| Dateien: |
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| Beitragende: | Prof. Dr. Jörg Pietruszka [Gutachter] Apl. Prof. Dr. Ulrich Schaffrath [Gutachter] | |||||||
| Dokumententyp (erweitert): | Dissertation | |||||||
| Dewey Dezimal-Klassifikation: | 500 Naturwissenschaften und Mathematik » 540 Chemie | |||||||
| Beschreibungen: | Dirigent- (DIR-) Proteine werden in unterschiedlichen Proteinuntergruppen (DIR-a bis DIR-i) eingeordnet. Sie werden vorwiegend im Pflanzenreich gefunden, dabei werden sie mit
unterschiedlichen adaptiven Reaktionen auf (a)biotische Stressfaktoren in Verbindung gebracht. Die ersten charakterisierten Mitglieder zeigten keine enzymatische Aktivität, konnten jedoch eine radikalische Dimerisierung (nach einer oxidativen Aktivierung) mit einer hohen Regio- und Enantioselektivität steuern. Trotz der Fähigkeit von DIR-Proteinen, pharmazeutisch relevante chirale Ausgangsstoffe zu produzieren, sind bisher kaum Anwendungsbeispiele etabliert. In der vorliegenden Arbeit wurden zwei Unterfamilien von DIR-Proteinen näher charakterisiert. Im ersten Teil wurden unterschiedliche Strategien angewendet, um die beiden DIR-a-Proteine (AtDIR6 und FiDIR1) heterolog und löslich in Escherichia coli (E. coli) zu produzieren. Demzufolge ergab die Kombination aus der Co-Expression von Chaperonen, niedrigen Temperaturen (15 °C) während der Überexpression und der Zugabe von 2 % Ethanol in das Kulturmedium die höchste Löslichkeit für die rekombinanten DIR-Proteine. Dadurch konnten zum ersten Mal lösliche rekombinante AtDIR6- und FiDIR1-Proteine hergestellt werden. Jedoch wiesen die Proteinfraktionen nach der Isolation eine hohe Verunreinigung mit Chaperonen und eine geringe Stabilität auf. Diese beiden Hindernisse müssten in weiteren Studien bearbeitet werden, um rekombinanten DIR-Proteine in der selektiven Kopplung von Lignanen nutzen zu können. Der Fokus dieser Arbeit lag in der biochemischen Charakterisierung eines chimären Jacalins OsJAC1 aus der monokotylen (einkeimblättrigen) Pflanze Reis (Oryza sativa). Dieses Protein ist modular aufgebaut aus einer Dirigent- (DIR-) und einer Jacalin-ähnlichen Lektin-(JRL-) Domäne. Das entsprechende Gen wird in Reaktion auf verschiedene abiotische und biotische Stimuli exprimiert. Durch die erfolgreiche heterologe Expression in E. coli mit hohen Ausbeuten für das Volllängenprotein OsJAC1 sowie seine einzelnen Domänenproteine (DIR und JRL) konnten die Proteine systematisch untersucht werden hinsichtlich der Struktur, der biochemischen Eigenschaften und der putativen Interaktionspartner. Dieser Ansatz ermöglichte es, verschiedene Analysemethoden anzuwenden, um neue spezifische Kohlenhydrat-Interaktionspartner für die beiden Domänen zu ermitteln. Es konnte gezeigt werden, dass die JRL-Domäne eine hohe Selektivität für Mannose und Glukose aufweist. Für die DIR-Domäne konnte zum ersten Mal eine Selektivität für Galaktose nachgewiesen werden. Zusätzlich konnte durch die Kristallisation des DIR-Domänenproteins im Komplex mit Galactobiose das neue Kohlenhydratbindemotiv ergründet werden. Durch unterschiedliche in silico (Protein-Protein-Docking) Untersuchungen, kombiniert mit weiteren biochemischen Untersuchungen (Schmelzpunkt, apparente Molekularmasse etc.) konnte ein erstes Modell für das Volllängenprotein erstellt werden. Die Ergebnisse in dieser Arbeit bieten Einblicke in die Strukturen und Bindungseigenschaften von OsJAC1 und seiner möglichen Funktion bei der Pathogenresistenz. Das Verständnis solcher Resistenzmechanismen gegen biotische Stressfaktoren und ihre Übertragung in moderne Züchtungsprogramme könnte den Weg zu einer umweltfreundlicheren Landwirtschaft unterstützen.Dirigent- (DIR-) proteins are divided into different protein subgroups (DIR-a to DIR-i) that are mainly found in the plant kingdom. They are associated with different adaptive responses to (a)biotic stresses. The first members of DIR proteins characterised showed no enzymatic activity but were able to control radical dimerization (after oxidative activation) with high regio- and stereoactivity. Despite the ability of DIR proteins to produce pharmaceutically relevant chiral precursors, only few examples of their application have been described. In the present work, two subfamilies of DIR proteins were examined in detail. In the first part, different strategies were used to produce two DIR-a proteins (AtDIR6 and FiDIR1) heterologous and soluble in Escherichia coli (E. coli). In this regard, the combination of chaperone co-expression, low temperatures (15 °C) during overexpression and the addition of 2% ethanol to the culture medium resulted in the highest solubility for the recombinant DIR proteins. This allowed the production of soluble recombinant AtDIR6 and FiDIR1 proteins for the first time. However, after isolation, the protein fractions showed high contamination with chaperones and low stability. These two obstacles would need to be addressed in further studies in order to use recombinant DIR proteins in the selective coupling of lignans. The focus of this work was the biochemical characterisation of the monocot chimeric jacalin (MCJ) OsJAC1 from Oryza sativa. This protein has a modular structure consisting of a dirigent (DIR) and a jacalin-like lectin (JRL) domain. The corresponding gene is expressed in response to various abiotic and biotic stimuli. Successful heterologous expression in E. coli with high yields for the full-length protein OsJAC1 and its individual domain proteins (DIR and JRL), allowed the proteins to be systematically studied in terms of structure, biochemical properties, and putative interaction partners. This approach made it possible to apply different analytical methods to identify new specific carbohydrate interaction partners for the two domains. The JRL domain was shown to be selective for mannose and glucose and, for the first time, galactose selectivity was demonstrated for the DIR domain. In addition, crystallisation of the DIR domain protein in complex with galactobiose allowed the new carbohydrate-binding motif to be explored. Through different in silico (protein-protein docking) investigations combined with further biochemical investigations (melting point, apparent molecular mass, etc.), a first model for the full-length protein could be established. The results in this work provide insights into the structures and binding properties of OsJAC1 and its possible function in the pathogen resistance mechanism. Understanding such resistance mechanisms against biotic stress factors and transferring them into modern breeding programmes could support the development of a more environmentally benign agriculture sector. | |||||||
| Quelle: | [1] D. Simpson, S. Amos, in Pharmacognosy, Elsevier, 2017, pp. 267-280.
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| Lizenz: |  Dieses Werk ist lizenziert unter einer Creative Commons Namensnennung 4.0 International Lizenz | |||||||
| Fachbereich / Einrichtung: | Mathematisch- Naturwissenschaftliche Fakultät » WE Chemie » Bioorganische Chemie | |||||||
| Dokument erstellt am: | 12.03.2024 | |||||||
| Dateien geändert am: | 12.03.2024 | |||||||
| Promotionsantrag am: | 24.11.2022 | |||||||
| Datum der Promotion: | 12.05.2023 |
