Publikationsserver der Universitätsbibliothek Marburg
Titel:Untersuchungen zur Struktur und Stabilität neuer, durch Genome Mining identifizierter Lassopeptide
Autor:Zimmermann, Marcel
Weitere Beteiligte: Marahiel, Mohamed A. (Prof. Dr.)
Veröffentlicht:2013
URI:https://archiv.ub.uni-marburg.de/diss/z2013/0721
URN: urn:nbn:de:hebis:04-z2013-07212
DOI: https://doi.org/10.17192/z2013.0721
DDC: Chemie
Titel (trans.):Structure and stability investigations of novel lasso peptides identified by genome mining
Publikationsdatum:2013-12-18
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Biosynthese, nuclear magnetic resonance, Naturstoff, Massenspektrometrie, Stabilität, Peptide, structure, Struktur, genome mining, stability, Magnetische Kernresonanz, Mutation, ribosomal peptide, genome mining

Zusammenfassung:
Das zunehmende Auftreten multiresistenter Bakterien macht die Suche nach neuen antibakteriellen Wirkstoffen notwendiger denn je. Naturstoffe stellen dabei eine sehr reichhaltige Quelle dar, da sie über strukturelle und chemische Diversität verfügen, die teilweise nicht oder nur unter großem Aufwand synthetisch zugänglich ist. Für die Identifikation neuer Naturstoffe kann dabei besonders die Methode des Genome Minings genutzt werden, da durch die stark gesunkenen Kosten von Sequenzierungen immer mehr Komplettgenome in den Datenbanken zur Verfügung stehen. Eine spezielle Familie der ribosomal synthetisierten und post-translational modifizierten Peptide (RiPPs) sind die Lassopeptide, die ihren Namen ihrer besonderen dreidimensionalen Faltung verdanken. Diese zeigen trotz geringer chemischer Modifikation thermische und proteolytische Stabilität und teilweise interessante Bioaktivitäten. In dieser Arbeit konnten mit dem Genome Mining Ansatz fast 100 potentielle Lassopeptidbiosynthesegencluster identifiziert werden. Als Beweis der Funktionalität des Genome Minings wurde ein Cluster ausgewählt und das hitzelabile Lassopeptid Astexin-1 in verschiedenen Verkürzungsvarianten isoliert, auf thermische und proteolytische Stabilität hin untersucht und seine 3D-Struktur mittels NMR-Spektroskopie aufgeklärt. Eine extensive Mutagenesestudie wurde zur Untersuchung der Spezifität der Biosynthesemaschinerie, sowie zur Identifikation wichtiger Reste für die Stabilität der Lassofaltung durchgeführt. Dabei konnte durch rationale Inkorporation einer Mutation der nativ hitzelabile Naturstoff in ein hitzestabiles Lassopeptid transformiert werden. Im zweiten Teil der Arbeit wurden zwei Biosynthesegencluster aus Caulobacter sp. K31, die durch Genome Mining identifiziert worden sind, ausgewählt und es konnten vier neue Lassopeptide, die Caulonodine IV – VII, isoliert werden. Diese vier Caulonodine tragen Serin bzw. Alanin an Position 1 der Lassopeptidsequenz und definieren damit die Klasse II der Lassopeptide neu, da vorher nur Peptide mit Glycin an dieser Position bekannt waren. Die Caulonodine wurden auf ihre thermische und proteolytische Stabilität hin untersucht und offenbarten sich als hitzelabile Lassopeptide. Die anschließende Mutagenesestudie zeigte die veränderte Spezifität der Biosynthesemaschinerie für Position 1 und ermöglichte die Postulierung der Stöpselaminosäuren für alle vier Caulonodine. Diese Vorhersage wurde für Caulonodin V durch Aufklärung der 3D Struktur mittels NMR-Spektroskopie bestätigt. Eine Mutagenesestudie des Leaderpeptids konnte bestätigen, dass im Leaderpeptid weitere Reste neben Thr-2 für die Prozessierung durch die Biosynthesemaschinerie wichtig sind.

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