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| The EMBO Journal
(1998) 17, 3640–3650, doi:10.1093/emboj/17.13.3640 |
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| Overlapping functions of components of a bacterial Sec-independent protein export pathway |
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| Frank Sargent1, 2, Erik G. Bogsch3, Nicola R. Stanley1, 2, Margaret Wexler1, 2, Colin Robinson3, Ben C. Berks2 and Tracy Palmer1, 2 |
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1 Nitrogen Fixation Laboratory, John Innes Centre, Colney, Norwich NR4 7UH, UK 2 Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK 3 Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK To whom correspondence should be addressed Tracy Palmer, PALMER@BBSRC.AC.UK Received 14 April 1998; Accepted 29 April 1998. |
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| Abstract |
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| 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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| Keywords: hydrogenases, molybdoenzymes, periplasm, Sec-independent protein export, twin arginine transfer peptide |
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