A common export pathway for proteins binding complex redox cofactors?
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.
Berks
B C
BC
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich, UK. b.berks@uea.ac.uk
D000595:Amino Acid Sequence; D001120:Arginine / Q000502:physiology*; D001419:Bacteria / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D021382:Protein Sorting Signals / Q000737:chemistry* / Q000502:physiology*; D015398:Signal Transduction
D021382:Protein Sorting Signals; D001120:Arginine