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SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm

van 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.

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DOI

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.

Original languageEnglish
Pages (from-to)619 - 629
Number of pages11
JournalMolecular Microbiology
Volume22
Issue number4
Publication statusPublished - Nov-1996

    Keywords

  • PROTEIN TRANSLOCATION, PLASMA-MEMBRANE, PRECURSOR PROTEIN, CYTOPLASMIC MEMBRANE, ACIDIC PHOSPHOLIPIDS, INNER MEMBRANE, TRIGGER FACTOR, BINDING, ATPASE, EXPORT

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