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Titel:Struktur und Funktion von Flokkulinen aus Saccharomyces cerevisiae sowie weiterer pilzlicher Zellwandproteine
Autor:Veelders, Maik Stefan
Weitere Beteiligte: Essen, Lars-Oliver (Prof. Dr.)
Veröffentlicht:2012
URI:https://archiv.ub.uni-marburg.de/diss/z2013/0051
URN: urn:nbn:de:hebis:04-z2013-00517
DOI: https://doi.org/10.17192/z2013.0051
DDC: Chemie
Titel (trans.):Structure and function of flocculins from Saccharomyces cerevisiae and other fungal cell wall proteins
Publikationsdatum:2013-02-20
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Flocculation, Kristallographie, Flokkulin, Adhäsin, Saccharomyces cerevisiae, Flokkulation, Domäne, Flocculin, Adhesin

Zusammenfassung:
Die Zellwand ist die primäre Interaktionsfläche von Hefezellen mit ihrer Umwelt. Sie besteht in ihrer inneren Schicht aus Chitin, β1,3- und β1,6-Glucanen, die für ihre Stabilität entscheidend sind. In der äußeren Schicht der Hefezellwand finden sich verschiedene Glyco-proteine, die für die Erkennung und Bindung von Zellen untereinander und die Interaktion mit ihrer weiteren Umgebung notwendig sind. Der Aufbau und Umbau der Zellwand selbst während des Zellzyklus der Hefe ist ein essentieller Vorgang, in den ebenfalls verschiedene Proteine, die in der Zellwand vorkommen und Glucane prozessieren, involviert sind. In dieser Arbeit wurden Adhäsine und das innere Zellwandprotein Sun4 aus der Bäckerhefe Saccharomyces cerevisiae und der humanpathogenen Hefe Candida glabrata strukturell und funktionell untersucht. Die untersuchten pilzlichen Adhäsine Flo5, Flo11 und Epa1 vermitteln vegetative Adhäsion der Hefen entweder an weitere Hefezellen, abiotische Substrate oder Wirtszellen. Sie bilden eine Familie mit einer gemeinsamen Superstruktur, die aus einer adhäsionsvermittelnden, N-terminalen A-Domäne, einer mittleren, hochglycosylierten B Domäne und einer C-terminalen C-Domäne mit Glycosylphosphatidylinositolanker besteht. In dieser Arbeit war es möglich, die molekularen Strukturen der adhäsionsvermittelnden Domänen Flo5A, Epa1A und Flo11A bei atomaren Auflösungen (0.89-1.5 Å) zu bestimmen. Dabei wurde deutlich, dass die mit der PA14-Domäne aus dem Anthrax-protektiven Antigen verwandten A-Domänen von Flo5 und Epa1 eine C-Typ-Lektin-artige Aktivität aufweisen und Glycanstrukturen auf anderen Hefezellen (Flo5A) oder Wirtszellen (Epa1A) binden. Native, für die biologische Funktion relevante Liganden konnten in den Strukturen beobachtet und Bindungskonstanten bestimmt werden. Die Flo11A-Domäne zeigt einen vollständig neuen Faltungstyp, offenbarte ihre Ligandspezifität jedoch nicht durch strukturelle Untersuchungen. Allerdings konnte ein lektinartiger Mechanismus ausgeschlossen und ein auf aromatischen Bändern beruhender, homotypischer Mechanismus vorgeschlagen werden. Die Struktur der in Pilzen hochkonservierten C-terminalen SUN-Domäne des inneren Zellwandproteins Sun4 aus S. cerevisiae konnte ebenfalls in atomarer Auflösung aufgeklärt und Hinweise auf eine β-Glucanase Aktivität dieser Domäne gefunden werden. Durch strukturbasiertes Design sollte die Entwicklung von fungiziden Medikamenten gegen diese in Pilzen ubiquitäre, aber exklusiv vorkommende Domäne möglich sein. Ein heterotypischer Gadolinium-Oxo-Supercluster, der während der Phasierung auf der Oberfläche von Flo5A beobachtet wurde, könnte als Templat für die Inkorporation von Gadolinium in verschiedene Proteine und so langfristig für die Entwicklung eines biokompatiblen und gewebespezifischen MRT-Kontrastmittels dienen.

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