Publikationsserver der Universitätsbibliothek Marburg
Titel:Analyse der subzellulären Lokalisation des C-Signalvorläuferproteins p25 und die Identifikation der PopC-Spaltstelle in p25 in Myxococcus xanthus
Autor:Ammon, Meike
Weitere Beteiligte: Søgaard-Andersen, Lotte (Prof.)
Veröffentlicht:2011
URI:https://archiv.ub.uni-marburg.de/diss/z2011/0078
DOI: https://doi.org/10.17192/z2011.0078
URN: urn:nbn:de:hebis:04-z2011-00780
DDC: Biowissenschaften, Biologie
Titel (trans.):Analysis of the subcellular localization of the C-signal precursor p25 and identification of the PopC cleavage site in p25 in Myxococcus xanthus
Publikationsdatum:2011-03-18
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
C-Signal, Proteolyse, Subtilase, Fruchtkörperbildung, Development, Myxococcus xanthus, Serinproteinasen

Zusammenfassung:
Myxococcus xanthus ist ein Bakterium, das ein außergewöhnliches Verhalten bei Nährstoffmangel zeigt. Im Zuge eines Entwicklungszyklus bilden diese Bakterien Fruchtkörper, die mit Dauerformen, den sogenannten Myxosporen gefüllt sind, um die lebensbedrohlichen Umweltbedingungen zu überstehen. Sechs Stunden nach Eintritt des Hungerzustandes koordiniert und reguliert das C Signal die Aggregation der Zellen zur Fruchtkörperbildung, die Sporulation der Zellen zu Myxosporen und eine spezifische Genexpression. Beim C Signal handelt es sich um das 17 kDa große Protein p17, welches nach der Prozessierung des C Signalvorläuferproteins p25 durch die Subtilisin-ähnliche Serinprotease PopC entsteht. In dieser Arbeit sollte zum einen die Orientierung von p25 in der äußeren Membran untersucht und zum anderen die PopC-Spaltstelle in p25 identifiziert werden. Um die subzelluläre Lokalisation von p25 zu untersuchen, wurden intakte Zellen mit einer unspezifischen Protease behandelt. Anschließend wurde in Immunoblot Analysen geprüft, ob p25 im Vergleich zu Kontrollproteinen degradiert wird. p25 zeigte ein identisches Verhalten wie das Kontrollprotein PilQ, ein Protein der äußeren Membran, welches auf der Zelloberfläche exponiert ist. Als weitere Kontroll-proteine dienten Tgl, ein Protein der äußeren Membran, das ins Periplasma ragt, und PilC, ein Protein der inneren Membran. Tgl und PilC wurden im Gegensatz zu PilQ und p25 weniger stark degradiert. Daher deuten die Ergebnisse darauf hin, dass p25 auf der Zelloberfläche exponiert ist. Um die PopC-Spaltstelle zu identifizieren, wurden biochemische und genetische Strategien verfolgt. Synthetische Peptide wurden herangezogen, um die PopC-Spaltung zu analysieren. Der N-Terminus von p17 sollte mittels Massenspektrometrie bestimmt werden. Außerdem wurde die Spaltung von verkürzten MalE-p25 Deletionsderivaten und Alaninsubstitutionsmutanten durch gereinigtes PopC Protein in vitro untersucht. Damit wurde das Spaltmotiv in p25 auf die Aminosäuren 56LDV58 eingegrenzt. Die Untersuchungen von Alanin-substitutionen in vitro und in vivo lassen schlussfolgern, dass Aspartat 57 essentiell für die PopC-Spaltung in M. xanthus ist. Daher deuten die Daten darauf hin, dass PopC p25 im Spaltmotiv 56LDV58 nach Aspartat 57 spaltet.

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