SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasmvan der Does, C., den Blaauwen, T., de Wit, J. G., Manting, E. H., Groot, N. A., Fekkes, P. & Driessen, A. J. M., Nov-1996, In : Molecular Microbiology. 22, 4, p. 619 - 629 11 p.
Research output: Contribution to journal › Article › Academic › peer-review
SecA is the dissociable ATPase subunit of the Escherichia coli preprotein translocase, and cycles in a nucleotide-modulated manner between the cytosol and the membrane. Overproduction of the integral subunits of the translocase, the SecY, SecE and SecG polypeptides, results in an increased level of membrane-bound SecA. This fraction of SecA is firmly associated with the membrane as it is resistant to extraction with the chaotropic agent urea, and appears to be anchored by SecYEG rather than by lipids, Topology analysis of this membrane-associated form of SecA indicates that it exposes a carboxy-terminal domain to the periplasmic face of the membrane.
|Pages (from-to)||619 - 629|
|Number of pages||11|
|Publication status||Published - Nov-1996|
- PROTEIN TRANSLOCATION, PLASMA-MEMBRANE, PRECURSOR PROTEIN, CYTOPLASMIC MEMBRANE, ACIDIC PHOSPHOLIPIDS, INNER MEMBRANE, TRIGGER FACTOR, BINDING, ATPASE, EXPORT