The 'trigger factor cycle' includes ribosomes, presecretory proteins, and the plasma membrane
| Autor: | Elliott Crooke, William Wickner, Roland Lill, Brenda Guthrie |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Ribosomal Proteins
Protein subunit Cell Ribosome Models Biological General Biochemistry Genetics and Molecular Biology Bacterial Proteins Cell surface receptor medicine Centrifugation Density Gradient Escherichia coli Protein Precursors 50S Amino Acid Isomerases Peptidylprolyl isomerase biology Escherichia coli Proteins Cell Membrane Biological Transport Peptidylprolyl Isomerase Cell biology Molecular Weight medicine.anatomical_structure Biochemistry Cytoplasm biology.protein Protein A Carrier Proteins Ribosomes Bacterial Outer Membrane Proteins |
| Zdroj: | Cell. 54(7) |
| ISSN: | 0092-8674 |
| Popis: | Trigger factor is a soluble, 63,000 dalton protein of E. coli that stabilizes proOmpA, the precursor form of a major outer-membrane protein, in a conformation competent for in vitro membrane assembly. There is approximately one trigger factor molecule bound to each 70S ribosome isolated from cell extracts in physiological buffers. Trigger factor dissociates from ribosomes in 1.5 M LiCl and reassociates with salt-washed ribosomes in low-salt buffer. Binding is exclusively to the 50S (large) subunit, known to contain the exit domain for nascent polypeptide chains. In addition to its associations with proOmpA and ribosomes, excess trigger factor can compete with the proOmpA-trigger factor complex for a limited number of membrane sites that are essential for translocation of proOmpA. These data suggest a model of trigger factor cycling between the cytoplasm, the ribosome, presecretory proteins, and membrane receptor proteins. |
| Databáze: | OpenAIRE |
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