A common export pathway for proteins binding complex redox cofactors?

B C Berks

doi:10.1046/j.1365-2958.1996.00114.x

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A common export pathway for proteins binding complex redox cofactors?

B C Berks

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Abstract

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.

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Amino Acid Sequence Arginine Bacteria Models, Biological Molecular Sequence Data Oxidation-Reduction Protein Sorting Signals Signal Transduction Journal Article Research Support, Non-U.S. Gov't Review

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B C Berks. 1996. A common export pathway for proteins binding complex redox cofactors?. https://doi.org/10.1046/j.1365-2958.1996.00114.x

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