SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm
Van Der Does, Chris ; Den Blaauwen, Tanneke ; De Wit, Janny G. ; Manting, Erik H. ; Groot, Nancy A. ; Fekkes, Peter ; Driessen, Arnold J. M.
Oxford BSL : Blackwell Science Ltd
Published 1996
Oxford BSL : Blackwell Science Ltd
Published 1996
| ISSN: |
1365-2958
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|---|---|
| Source: |
Blackwell Publishing Journal Backfiles 1879-2005
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| Topics: |
Biology
Medicine
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| Notes: |
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.
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| Type of Medium: |
Electronic Resource
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| URL: |