Now showing items 1-5 of 5
Nachweis und Analyse BamA-assoziierter Faltungsintermediate des OmpA durch ortsgerichtete Fluoreszenzspektroskopie
Die Faltung und Insertion von Außenmembranproteinen (OMPs) in die Außenmembran von Gram negativen Bakterien ist für das Leben der Zellen essentiell und erfordert den konservierten β-barrel assembly machinery (BAM) Komplex. Zahlreiche Studien befassen sich mit der Aufklärung des dahinterstehenden Faltungsmechanismus von OMPs, doch bislang ist nur sehr wenig darüber bekannt. Daher steht der Faltungsmechanismus der spontanen Faltung und Insertion von OMPs wie OmpA und der Einfluss der BAM Hauptkomponente BamA darauf, ...
The periplasmic domain of the barrel assembly machinery protein A (BamA) from Escherichia coli assists folding of outer membrane protein A
The assembly of outer membranes of the cell wall of Gram-negative bacteria and of various organelles of eukaryotic cells requires the evolutionarily conserved β-barrel-assembly machinery (BAM) complex. This thesis describes the biochemical and biophysical properties of the periplasmic domain of the β-barrel assembly machinery protein A (PD-BamA) of the E. coli BAM complex, its effect on insertion and folding of the Outer membrane protein A (OmpA) into lipid bilayers and the identification of regions of PD-BamA that ...
Facilitating folding of outer membrane proteins, roles of the periplasmic chaperone Skp and the outer membrane lipoprotein BamD
This thesis describes several important advancements in the understanding of the assembly of outer membrane proteins of Gram-negative bacteria like Escherichia coli. A first study was performed to identify binding regions in the trimeric chaperone Skp for outer membrane proteins. Skp is known to facilitate the passage of unfolded outer membrane proteins (OMPs) through the periplasm to the outer membrane (OM). A gene construct named “synthetic chaperone protein (scp)” gene was used to express a fusion protein (Scp) ...
Association of neighboring β-Strands to form the β-barrel structure of the voltage-dependent anion channel, human isoform 1 (hVDAC1) precedes membrane insertion and is largely driven by polar interactions between basic and acidic amino acid side-chains
To date, all biophysical folding studies on β-barrel membrane proteins from outer membranes (OMPs) indicated a coupled mechanism of folding and membrane insertion. Most of these studies were performed with smaller OMPs from bacteria. Here we have investigated folding and insertion of a mitochondrial OMP, the voltage-dependent anion-selective channel (VDAC), human isoform 1 (hVDAC1). To examine whether folding and insertion are coupled for hVDAC1, the association of neighboring β-strands of the 19-stranded β-barrel ...
BamB facilitates folding of outer membrane protein A (OmpA) via interactions of its β-propeller with the membrane surface and via a conformation change induced by phosphatidylglycerol
A sufficient folding and insertion of OMPs into the OM of Gram-negative bacteria requires the conserved β-barrel assembly machinery (BAM) complex. The present thesis concerns the structural properties and folding behavior of the lipoprotein BamB and describes its relevance in the synchronized mechanism of membrane insertion and folding of the β-barrel protein OmpA. Furthermore, specific binding sites in BamB involved in the interaction to the lipid membrane or the periplasmic domain of BamA (PD-BamA) were identified ...