A cell-free protein translocation system prepared entirely from a Gram-positive organism
| Autor: | Karl-Ludwig Schimz, Gaby Decker, Elke Frings, Jochen Meens, Matthias Müller, Michael Klein |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
SecA
Staphylococcus medicine.medical_treatment Molecular Sequence Data Biophysics Chromosomal translocation Biochemistry Bacterial Proteins Structural Biology Genetics medicine Staphylococcus carnosus Cell-free translocation system Molecular Biology Staphylococcus hyicus Adenosine Triphosphatases Enzyme Precursors SecA Proteins Protease Base Sequence biology Chemistry Escherichia coli Proteins Vesicle Cell Membrane Serine Endopeptidases Membrane Transport Proteins Biological Transport Lipase Cell Biology Gram-positive bacteria biology.organism_classification Cytosol Secretory protein Cytoplasm Protein secretion Endopeptidase K SEC Translocation Channels |
| Zdroj: | FEBS Letters. 362:29-33 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(95)00180-h |
| Popis: | A cell-free protein translocation system derived exclusively from a Gram-positive bacterium is described here for the first time. Highly efficient in vitro synthesis of plasmid encoded preprolipase of Staphylococcus hyicus is accomplished by coupled transcription/translation using either a cytosolic extract of S. carnosus alone or in combination with T7-RNA-polymerase. Addition of inside-out cytoplasmic membrane vesicles of S. carnosus leads to the partial conversion (processing) of preprolipase to prolipase. In addition, as shown in a protease protection assay, a significant part of preprolipase plus prolipase is translocated in vitro into the lumen of the vesicles. Translocation of preprolipase into the membrane vesicles requires the proton-motive force and the S. carnosus SecA protein. |
| Databáze: | OpenAIRE |
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