Abstract
A high‐expression plasmid for the secA gene was constructed. The SecA protein was then overproduced in E. coli and purified. The purified SecA stimulated the in vitro translocation of a model secretory protein into inverted membrane vesicles pretreated with 4 M urea. Membrane vesicles from a secAts mutant exhibited lower translocation activity, which was enhanced by SecA. These results indicate that SecA is directly involved in protein secretion across the cytoplasmic membrane.
References
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 3:45 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 17, 2023, 2:52 a.m.) |
Indexed | 1 year, 1 month ago (July 22, 2024, 4:27 p.m.) |
Issued | 36 years, 8 months ago (Jan. 2, 1989) |
Published | 36 years, 8 months ago (Jan. 2, 1989) |
Published Online | 23 years, 10 months ago (Oct. 19, 2001) |
Published Print | 36 years, 8 months ago (Jan. 2, 1989) |
@article{Kawasaki_1989, title={SecA protein is directly involved in protein secretion in Escherichia coli}, volume={242}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(89)80516-2}, DOI={10.1016/0014-5793(89)80516-2}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Kawasaki, Hisashi and Matsuyama, Shin-ichi and Sasaki, Shoichi and Akita, Mitsuru and Mizushima, Shoji}, year={1989}, month=jan, pages={431–434} }