Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 14 of 14 for “"twin-arginine"”.
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Mapping protein-protein interactions in the <i>Escherichia coli</i> Twin Arginine Translocase
The Twin Arginine Translocase (Tat) system is a membrane-bound transport system present in plants and bacteria that has the remarkable ability to export fully folded proteins across a lipid bilayer, powered by the protonmotive force. In Escherichia coli the Tat system is composed of only three …
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Caracterización del sistema TAT (Twin Arginine Translocation) de transporte de proteínas en Rhizobium leguminosarum bv viciae UPM791
… bacterias un sistema alternativo denominado TAT (Twin arginine Translocation) que depende de fuerza protón-motriz y reconoce proteínas con un péptido señal caracterizado por la presencia de la secuencia consenso S/TRRxFLX en la que la doble arginina está presente en la mayoría de los casos y los …
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A nucleic acid-based bacterial message export system for cell-to-cell communication
… cellular machinery. Exploiting the bacterial twin-arginine translocation (TAT) pathway and a nucleic-acid binding protein sourced from bacteriophage MS2, we have engineered a message-sending system in Escherichia coli capable of specifically exporting a "pre-written" circularized RNA message …
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Konstruktion eines bakteriellen Systems zum Export von Coenzym B<sub>12</sub>
… erfolgte über den Signalsequenz-abhängigen Tat ( twin arginine translocation")-Transportweg, der native Enzyme mit gebundenem Kofaktor wie z. B. die Trimethylamin-N-Oxid-Reduktase (TorA) aus Escherichia coli exportiert. Für die Konstruktion des B12-Exporters wurde die Tat-Signalsequenz von TorA …
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The dual-targeted membrane assembly of the <i>Streptomyces coelicolor</i> Rieske protein
… - the general secretory (Sec) system and the twin-arginine translocation (Tat) system. Both translocases can also insert membrane proteins. The Sec machinery inserts multiple transmembrane domains into the cytoplasmic membrane by a co-translational mechanism, whereas, the Tat machinery …
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Probing the role of Tat proofreading chaperones in the assembly of molybdoenzymes
<br/>The twin-arginine (Tat) system is a specialised translocation machine found in prokaryotes and chloroplasts which serves to export fully folded proteins across the cytoplasmic membrane. Proteins are specifically targeted to this system by N-terminal signal peptides which bear a conserved …
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Novel Cell Surface Anchoring Mechanism Of Prokaryotic Secreted Protein
… across the H. volcanii membrane via the Twin Arginine (Tat) pathway demonstrating that Sec and Tat substrates can be C-terminally processed in an ArtA-dependent manner. Considering that ArtA homologs are conserved among diverse organisms of both prokaryotic domains, data obtained from my …
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Der Proteintransport in Rhodobacter capsulatus und Escherichia coli über das Tat-Transportsystem
… werden sie posttranslational über den Tat-Weg (twin arginine translocation) in das Periplasma transloziert. Charakteristisch für die Tat-Substrate ist das Doppelarginin-haltige S-R-R-x-F-L-K-Konsensusmotiv in der Signalsequenz. Das Tat-Translokon wird in E. coli von den Membranproteinen TatA, …
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Interactions between the TatBC complex and Tat signal peptides during protein transport by the bacterial Tat pathway
… They critically contain an almost invariant twin-arginine (RR) motif within the n-region that is essential to trigger Tat transport. Tat signal peptides interact with the Tat receptor complex that contains multiple copies of TatA, TatB and TatC, probably in 1:1:1 ratio. Substrate binding at …
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Periplasmic determinants of virulence in Salmonella enterica
… to be exported, it would be transported via the Twin Arginine Transport (Tat) system, which translocates folded proteins into the periplasm. This transport system is important for virulence in mice, but it is not needed for most growth conditions in the laboratory. I found that SodCI does not …
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Investigations into the roles of bacterial TorD family chaperone proteins
The twin-arginine translocase (Tat) is a highly specialised protein transport system, present in prokaryotes and plant chloroplasts. This translocase functions to transport proteins across the cytoplasmic membrane in a fully folded state. Substrates of the Tat system are targeted to the system by …
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Holin-dependent secretion of a large clostridial cytotoxin by C. perfringens
… membrane topology to TatA, a key protein in the Twin Arginine Transport (Tat) secretion system. This thesis tests two models, a pore-forming model and a membrane destabilization model that may explain the mechanism behind TpeE-dependent secretion of TpeL in C. perfringens. The pore-forming model …
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Tat signal peptide recognition during protein maturation and export
… an N-terminal signal peptide harbouring a Tat (twin-arginine translocation) motif, which follows closely the consensus S/T-R-R-x-F-L-K. As with other proteins transported via the Tat pathway, NapA needs to be fully folded, and cofactor insertion needs to be completed, prior to export. This is …
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Probing the organisation of the TatC component in the Tat system of <i>Escherichia coli</i>
The Tat protein export system transports folded proteins across the bacterial cytoplasmic membrane and the plant thylakoid membrane. In Escherichia coli, the Tat system is composed of the TatA, TatB and TatC proteins. TatB and TatC assemble into a multimeric receptor complex that recognises and …