A common export pathway for proteins binding complex redox cofactors?
Article first published online: 31 OCT 2003
Blackwell Science Ltd, Oxford
Volume 22, Issue 3, pages 393–404, November 1996
How to Cite
Berks, B. C. (1996), A common export pathway for proteins binding complex redox cofactors?. Molecular Microbiology, 22: 393–404. doi: 10.1046/j.1365-2958.1996.00114.x
- Issue published online: 31 OCT 2003
- Article first published online: 31 OCT 2003
- Cited By
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.