SecA protein is required for secretory protein translocation into E. coli membrane vesicles
| Autor: | Lingling Chen, Robert J. Cabelli, Donald Oliver, Phang C. Tai |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Membranes
Mutant Chromosomal translocation Biological membrane Biology Alkaline Phosphatase medicine.disease_cause environment and public health Translocation Genetic General Biochemistry Genetics and Molecular Biology Organophosphorus Compounds Secretory protein Bacterial Proteins Biochemistry Affinity chromatography Mutation Escherichia coli medicine bacteria Alkaline phosphatase Protein Processing Post-Translational SEC Translocation Channels |
| Zdroj: | Cell. 55:683-692 |
| ISSN: | 0092-8674 |
| Popis: | The soluble and membrane components of an E. coli in vitro protein translocation system prepared from a secA amber mutant, secA13[Am], contain reduced levels of SecA and are markedly defective in both the cotranslational and posttranslational translocation of OmpA and alkaline phosphatase into membrane vesicles. Moreover, the removal of SecA from soluble components prepared from a wild-type strain by passage through an anti-SecA antibody column similarly abolishes protein translocation. Translocation activity is completely restored by addition of submicrogram amounts of purified SecA protein, implying that the observed defects are solely related to loss of SecA function. Interestingly, the translocation defect can be overcome by reconstitution of SecA into SecA-depleted membranes, suggesting that SecA is an essential, membrane-associated translocation factor. |
| Databáze: | OpenAIRE |
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