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The precursor polypeptides of periplasmic proteins binding seven types of redox cofactor have unusually long signal sequences bearing a consensus (S/T)-R-R-x-F-L-K motif immediately before the hydrophobic region. Such "double-arginine' signal sequences are not, in general, found on the precursors of other periplasmic proteins. It is suggested that precursor proteins with double-arginine signal sequences share a common specialization in their export pathway. The nature of this specialization, the structure of the double-arginine signal sequences, and the possible relationship with the double-arginine signal peptide-dependent thylakoid import pathway are discussed.

Original publication




Journal article


Mol Microbiol

Publication Date





393 - 404


Amino Acid Sequence, Arginine, Bacteria, Models, Biological, Molecular Sequence Data, Oxidation-Reduction, Protein Sorting Signals, Signal Transduction