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      TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli

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          Abstract

          The Tat (twin arginine translocation) system transports folded proteins across bacterial and thylakoid membranes. The integral membrane proteins TatA, TatB, and TatC are the essential components of the Tat pathway in Escherichia coli. We demonstrate that formation of a stable complex between TatB and TatC does not require TatA or other Tat components. We show that the TatB and TatC proteins are each able to a form stable, defined, homomultimeric complexes. These we suggest correspond to structural subcomplexes within the parental TatBC complex. We infer that TatC forms a core to the TatBC complex on to which TatB assembles.

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          Most cited references28

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          Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels.

          B Miroux, J. Walker (1996)
          We have investigated the over-production of seven membrane proteins in an Escherichia coli-bacteriophage T7 RNA polymerase expression system. In all seven cases, when expression of the target membrane protein was induced, most of the BL21(DE3) host cells died. Similar effects were also observed with expression vectors for ten globular proteins. Therefore, protein over-production in this expression system is either limited or prevented by bacterial cell death. From the few survivors of BL21(DE3) expressing the oxoglutarate-malate carrier protein from mitochondrial membranes, a mutant host C41(DE3) was selected that grew to high saturation cell density, and produced the protein as inclusion bodies at an elevated level without toxic effect. Some proteins that were expressed poorly in BL21(DE3), and others where the toxicity of the expression plasmids prevented transformation into this host, were also over-produced successfully in C41(DE3). The examples include globular proteins as well as membrane proteins, and therefore, strain C41(DE3) is generally superior to BL21(DE3) as a host for protein over-expression. However, the toxicity of over-expression of some of the membrane proteins persisted partially in strain C41(DE3). Therefore, a double mutant host C43(DE3) was selected from C41(DE3) cells containing the expression plasmid for subunit b of bacterial F-ATPase. In strain C43(DE3), both subunits b and c of the F-ATPase, an alanine-H(+) symporter, and the ADP/ATP and the phosphate carriers from mitochondria were all over-produced. The transcription of the gene for the OGCP and subunit b was lower in C41(DE3) and C43(DE3), respectively, than in BL21(DE3). In C43(DE3), the onset of transcription of the gene for subunit b was delayed after induction, and the over-produced protein was incorporated into the membrane. The procedure used for selection of C41(DE3) and C43(DE3) could be employed to tailor expression hosts in order to overcome other toxic effects associated with over-expression.
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            Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form.

            Hermann Schägger, Gebhard von Jagow (1991)
            A discontinuous electrophoretic system for the isolation of membrane proteins from acrylamide gels has been developed using equipment for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Coomassie dyes were introduced to induce a charge shift on the proteins and aminocaproic acid served to improve solubilization of membrane proteins. Solubilized mitochondria or extracts of heart muscle tissue, lymphoblasts, yeast, and bacteria were applied to the gels. From cells containing mitochondria, all the multiprotein complexes of the oxidative phosphorylation system were separated within one gel. The complexes were resolved into the individual polypeptides by second-dimension Tricine-SDS-PAGE or extracted without SDS for functional studies. The recovery of all respiratory chain complexes was almost quantitative. The percentage recovery of functional activity depended on the respective protein complex studied and was zero for some complexes, but almost quantitative for others. The system is especially useful for small scale purposes, e.g., separation of radioactively labeled membrane proteins, N-terminal protein sequencing, preparation of proteins for immunization, and diagnostic studies of inborn neuromuscular diseases.
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              Overlapping functions of components of a bacterial Sec-independent protein export pathway.

              Ben Berks, Brianna N. Stanley, F Sargent … (1998)
              We describe the identification of two Escherichia coli genes required for the export of cofactor-containing periplasmic proteins, synthesized with signal peptides containing a twin arginine motif. Both gene products are homologous to the maize HCF106 protein required for the translocation of a subset of lumenal proteins across the thylakoid membrane. Disruption of either gene affects the export of a range of such proteins, and a complete block is observed when both genes are inactivated. The Sec protein export pathway was unaffected, indicating the involvement of the gene products in a novel export system. The accumulation of active cofactor-containing proteins in the cytoplasm of the mutant strains suggests a role for the gene products in the translocation of folded proteins. One of the two HCF106 homologues is encoded by the first gene of a four cistron operon, tatABCD, and the second by an unlinked gene, tatE. A mutation previously assigned to the hcf106 homologue encoded at the tatABCD locus, mttA, lies instead in the tatB gene.
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                Author and article information

                Journal
                Journal ID (nlm-ta): FEBS Lett
                Journal ID (iso-abbrev): FEBS Lett
                Title: Febs Letters
                Publisher: Elsevier Science B.V
                ISSN (Print): 0014-5793
                ISSN (Electronic): 1873-3468
                Publication date PMC-release: 21 August 2007
                Publication date (Print): 21 August 2007
                Volume: 581
                Issue: 21
                Pages: 4091-4097
                Affiliations
                [a ]Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
                [b ]Department of Molecular Microbiology, The John Innes Centre, Norwich NR4 7UH, United Kingdom
                [c ]School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom
                [d ]Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom
                Author notes
                [* ]Corresponding author. Fax: +44 0 1865 275259. ben.berks@ 123456bioch.ox.ac.uk
                [1]

                Present address: Division of Molecular and Environmental Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.

                Article
                Publisher ID: FEBS31941
                DOI: 10.1016/j.febslet.2007.07.044
                PMC ID: 2517984
                PubMed ID: 17686475
                SO-VID: 085e24d9-2174-4688-b58e-7bd301ae853b
                Copyright © © 2007 Elsevier B.V.
                License:

                This document may be redistributed and reused, subject to certain conditions.

                History
                Date received : 22 May 2007
                Date revision received : 6 July 2007
                Date accepted : 19 July 2007
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular biology
                Keywords: membrane proteins,blue native-page,twin arginine,protein transport,bn-page, blue native-polyacrylamide gel electrophoresis,tat
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: membrane proteins, blue native-page, twin arginine, protein transport, bn-page, blue native-polyacrylamide gel electrophoresis, tat

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