Insbesondere in Organismen, die kein CaM haben, eröffnet sich aufgrund der strukturellen Identität von GlpD- und CaM- Bindemotiven eine neue experimentelle Strategie, um nach prokaryontischen Membranbindeproteinen zu suchen und diese näher zu charakterisieren.
Im Fall von GlpD wurde dies bereits erfolgreich demonstriert und kann auch bei anderen prokaryontischen CaM-Bindeproteinen angewandt werden. So ist z.B. ein Bereich des CaM-Bindeproteins GlpC hoch konserviert mit der GlpD-Membran-Insertionsdomäne (Abb.27). Durch Sekundärstrukturvorhersageprogramme wie PHD (Rost et al., 1994) und Predator (Rost et al., 1994) wurde für die Aminosäuren in diesem homologen Bereich von GlpC eine basische α-Helix mit amphiphilen Eigenschaften (Eisenberg et al., 1984) ermittelt (Abb30). Ferner wurde gezeigt, dass das CaM-Bindeprotein SecA in anionische Phospholipide inseriert (Breukink et al., 1992) und dass hierfür 70 Aminosäuren des C-Terminus von SecA essentiell sind (Breukink et al., 1995). Über Sekundärstrukturvorhersage-programme wie PHD und Predator wurde eine basisch amphiphile α-Helix im Bereich von Aminosäure 622-635 ermittelt, die mit CaM interagieren und in anionische Phospholipide inserieren könnte. Sekundärstrukturvorhersagen für das CaM-Bindeprotein TraC ermittelten eine basisch amphiphile Helix im Bereich von Aminosäuren 421-434 (Abb. 30).
Diskussion
Abb. 30: Basisch amphiphile Helices von GlpC, TraC und SecA als potentielle CaM- und Membran-bindedomänen. Die Graustufen entsprechen dem Hydrophobizitätsgrad der Aminosäuren, wobei die Aminosäuren mit größerer Hydrophobizität dunkler und hydrophilere Reste heller dargestellt sind.
Ob diese Helices für die CaM-Bindung essentiell sind, könnte durch CaM-Bindetests geprüft werden. CaM-Bindetests haben in experimenteller Hinsicht einige Vorteile gegenüber Monolayer- oder Liposomenbindungstests. Der erste Vorteil betrifft die experimentellen Voraussetzungen. So muss die Reinigung peripherer Membranproteine für CaM-Bindetests im Gegesatz zu Lipidmonolayer- bzw. Liposomenbindungstests nicht ohne den Einsatz von Detergenzien durchgeführt werden. Folglich erhält man für CaM-Bindetests eine höhere Ausbeute an Protein. Zweitens sind CaM-Bindetests experimentell einfacher durchzuführen, da keine speziellen Geräte (z.B. Mikro-Cahn-Waage) benötigt werden und sie nicht so sensitiv gegenüber externen Störungen (elektromagnetische Anziehung, Luftdruck etc.) sind wie Monolayer-Experimente. Drittens sind CaM-Bindetests nicht so zeitaufwendig, denn CaM-Sepharose wird industriell hergestellt und ist somit direkt einsetzbar. Für Liposomen-Bindungstests muss man dagegen die Liposomen erst herstellen.
CaM-Bindetests vereinfachen also die Suche nach peripheren Membranbindeproteinen bzw. -domänen und können als Screeningsystem in E. coli angewandt werden. Die Suche
A L
Diskussion
Identifizierung von Proteinen, die möglicherweise an Mikrodomänen lokalisiert sind, können CaM-Bindetests effizient eingesetzt werden.
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