title: SecA protein is directly involved in protein secretion in Escherichia coli.
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.
authors.affiliation: Institute of Applied Microbiology, University of Tokyo, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Kawasaki
authors.forename: S
authors.initials: S
authors.lastname: Matsuyama
authors.forename: S
authors.initials: S
authors.lastname: Sasaki
authors.forename: M
authors.initials: M
authors.lastname: Akita
authors.forename: S
authors.initials: S
authors.lastname: Mizushima
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D066298:In Vitro Techniques; D010957:Plasmids
chemical_list: D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins