Overlapping functions of components of a bacterial Sec-independent protein export pathway

Frank Sargent, Erik G. Bogsch, Nicola R. Stanley, Margaret Wexler, Colin Robinson, Ben C. Berks, Tracy Palmer

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    448 Citations (Scopus)


    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.
    Original languageEnglish
    Pages (from-to)3640-3650
    Number of pages11
    JournalEMBO Journal
    Issue number13
    Publication statusPublished - 1998


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