Publikationsserver der Universitätsbibliothek Marburg
Titel:Strukturbasierte Charakterisierung von Klasse II CPD Photolyasen
Autor:Kiontke, Stephan
Weitere Beteiligte: Essen, Lars-Oliver (Prof. Dr.)
Veröffentlicht:2012
URI:https://archiv.ub.uni-marburg.de/diss/z2013/0246
URN: urn:nbn:de:hebis:04-z2013-02463
DOI: https://doi.org/10.17192/z2013.0246
DDC:540 Chemie
Titel (trans.):Structure-based characterization of class II CPD photolyases
Publikationsdatum:2013-05-28
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Flavine, Antenna chromophore, UV-induzierte DNA-Schäden, Antennenchromophor, Rekombinantes Protein, Class II CPD photolyases, Deoxyribodipyrimidin-Photolyase, Protein crystallography, Methanosarcina mazei, Proteinkristallographie, Deazaflavine, Klasse II CPD Photolyasen, Structural biology, Strukturbiologie, Kristallstrukturanalyse, UV-induced DNA lesions, DNS-Reparatur, Or

Zusammenfassung:
CPD-Photolyasen sind substratspezifische, lichtgetriebene DNA-Reparaturenzyme, die mit der Energie des Sonnenlichts (300 nm – 500 nm) den UV-induzierten Hauptschaden im Erbgut, das Cyclobutanpyrimidindimer (CPD), entfernen und somit die genomische Integrität sicherstellen. Diese monomeren Enzyme besitzen neben dem katalytisch essentiellen Kofaktor FAD in der Regel einen zusätzlichen Antennenchromophor zur Erweiterung ihres Aktionsspektrums. Die Klassifizierung der CPD-Photolyasen erfolgt anhand von Sequenzhomologien und spiegelt sich bemerkenswerterweise auch im differenzierten Auftreten innerhalb der Lebewesen wider. Während der umfangreich charakterisierte Klasse I Subtyp auf mikrobielle Organismen beschränkt ist, existiert der weitgehend unerforschte Klasse II Subtyp ubiquitär in Pflanzen, Tieren, Bakterien, Archaeen sowie in einigen Viren. In dieser Arbeit erfolgte die funktionelle als auch strukturelle Charakterisierung des Klasse II Subtyps am Beispiel der Photolyasen aus der archaealen Gattung Methanosarcina. Diese Enzyme stellen aufgrund der hohen Sequenzhomologien zu den pflanzlichen und tierischen Orthologen geeignete Modelle für die Untersuchung eukaryotischer, Klasse II-spezifischer Aspekte dar. Die in dieser Arbeit gelösten Kristallstrukturen der Methanosarcina mazei Photolyase (MmCPDII) allein und im Komplex mit doppelsträngiger, CPD-geschädigter DNA lieferten die ersten dreidimensionalen Informationen für diese phylogenetisch distinkte Gruppe. Dabei wurde deutlich, dass der durch Gelshift-Experimente ermittelte geringe Diskriminierungsgrad zwischen ungeschädigter und geschädigter DNA des Klasse II Subtyps auf einen unterschiedlichen DNA Bindungsmodus zurückzuführen ist. Katalytische Merkmale ähneln zwar dem Klasse I Subtyp funktionell, unterscheiden sich aber auf struktureller Ebene und deuten so auf deren konvergente Evolution hin. So findet der Elektronentransport während der Photoreduktion des Kofaktors FAD ebenfalls entlang konservierter Tryptophane statt, nimmt aber eine neue Route und besteht nicht aus einer Triade, sondern aus einer Dyade mit mehreren terminalen Verzweigungspunkten. Vergleichbar mit dem Klasse I Subtyp erfolgt die Stabilisierung des neutralen semichionoiden Zustands während der Photoreduktion und der DNA Reparatur über ein Asparagin, das sich allerdings im Klasse II Subtyp konserviert auf einem anderen Strukturelement befindet. Mit Hilfe ortsgerichteter Mutagenese und UV/Vis-spektroskopischer Methoden war es möglich, die Funktion und Relevanz dieser Klasse II-spezifischen Merkmale zu verifizieren. Die Etablierung eines artifiziellen Synthesewegs zur Bereitstellung des Deazaflavins 8-HDF im Expressionswirt Escherichia coli identifizierte in letzter Konsequenz den anfänglich unbekannten Antennenchromophor der MmCPDII. Die Kristallstruktur des MmCPDII/8-HDF Komplexes wiederum lieferte detaillierte Einblicke in die Antennenbindungstasche und ermöglichte Schlussfolgerungen bezüglich potentieller Antennen für den gesamten Klasse II Subtyp, insbesondere für die pflanzlichen Photolyasen. Diese Informationen können einen wichtigen Beitrag zur Entdeckung des bisher kryptischen Antennenchromophors in pflanzlichen Photolyasen leisten.

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