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A common export pathway for proteins binding complex redox cofactors?

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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular Microbiology Wiley

A common export pathway for proteins binding complex redox cofactors?

Molecular Microbiology , Volume 22 (3) – Nov 1, 1996

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References (88)

Publisher
Wiley
Copyright
Blackwell Science Ltd, Oxford
ISSN
0950-382X
eISSN
1365-2958
DOI
10.1046/j.1365-2958.1996.00114.x
pmid
8939424
Publisher site
See Article on Publisher Site

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.

Journal

Molecular MicrobiologyWiley

Published: Nov 1, 1996

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