Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping
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The twin-arginine transport (Tat) system is dedicated to the translocation of folded proteins across the bacterial cytoplasmic membrane. Proteins are targeted to the Tat system by signal peptides containing a twin-arginine motif. In Escherichia coli, many ...
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The genus Desulfitobacterium belong to the low-GC gram-positive phylogenic group and is a versatile obligate anaerobe capable of reducing very diverse terminal electron acceptors such as sulfite, nitrate, fumarate, thiosulfate, and a few polluting chlorina ...
The twin-arginine translocation (Tat) system is a bacterial protein targeting pathway. Tat-targeted proteins display signal peptides containing a distinctive SRRxFLK ‘twin-arginine’ motif. The Escherichia coli trimethylamine N-oxide reductase (TorA) bears ...
The Golgi complex (GC) represents the central junction for membrane trafficking. Protein and lipid cargoes continuously move through the GC in both anterograde and retrograde directions, departing to and arriving from diverse destinations within the cell. ...
Membrane protein research depends largely on the availability of functional protein in an instrumental set- up for application of biophysical investigations. We used an in vitro synthesis strategy in the presence of a solid supported lipid membrane as a ne ...
Membrane protein research depends largely on the availability of functional protein in an instrumental set-up for application of biophysical investigations. We used an in vitro synthesis strategy in the presence of a solid supported lipid membrane as a new ...
