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SecA protein is required for secretory protein translocation into E. coli membrane vesicles
| Content Provider | Semantic Scholar |
|---|---|
| Author | Cabelli, R. J. Chen, Lingling Tai, Phang C. Oliver, Donald B. |
| Copyright Year | 1988 |
| Abstract | 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. |
| Starting Page | 683 |
| Ending Page | 692 |
| Page Count | 10 |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/0092-8674(88)90227-9 |
| PubMed reference number | 2846186 |
| Journal | Medline |
| Volume Number | 55 |
| Alternate Webpage(s) | https://api.elsevier.com/content/article/pii/0092867488902279 |
| Alternate Webpage(s) | https://www.sciencedirect.com/science/article/pii/0092867488902279?dgcid=api_sd_search-api-endpoint |
| Alternate Webpage(s) | https://doi.org/10.1016/0092-8674%2888%2990227-9 |
| Journal | Cell |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
