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Science 11 July 1986:
Vol. 233. no. 4760, pp. 206 - 208
DOI: 10.1126/science.2941862
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Articles

Science, Vol 233, Issue 4760, 206-208
Copyright © 1986 by American Association for the Advancement of Science

articles

Conformations of signal peptides induced by lipids suggest initial steps in protein export

MS Briggs, DG Cornell, RA Dluhy, and LM Gierasch

Despite the requirement for a functional signal sequence in protein export, little is known of the conformational properties and membrane interactions of these highly hydrophobic amino terminal extensions on nearly all exported proteins. The Escherichia coli lambda phage receptor signal sequence was studied in phospholipid monolayers by circular dichroism and Fourier transform infrared spectroscopy; the signal peptide was shown to prefer an alpha-helical conformation when inserted into the lipid phase. However, interaction with the lipid surface without insertion induced the signal sequence, which is unstructured in bulk aqueous solution, to adopt a beta structure. These observations are combined in a model for the initial steps in signal sequence-membrane interaction in vivo.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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The Conformation of a Signal Peptide Bound by Escherichia coli Preprotein Translocase SecA.
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Interactions of the Human Calcitonin Fragment 9-32 with Phospholipids: A Monolayer Study.
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Proteomics of Protein Secretion by Bacillus subtilis: Separating the "Secrets" of the Secretome.
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Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?.
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Signal Peptide-Dependent Protein Transport in Bacillus subtilis: a Genome-Based Survey of the Secretome.
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Membrane-bound state of the colicin E1 channel domain as an extended two-dimensional helical array.
S. D. Zakharov, M. Lindeberg, Y. Griko, Z. Salamon, G. Tollin, F. G. Prendergast, and W. A. Cramer (1998)
PNAS 95, 4282-4287
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In Vitro Interaction between a Chloroplast Transit Peptide and Chloroplast Outer Envelope Lipids Is Sequence-specific and Lipid Class-dependent.
P. Pinnaduwage and B. D. Bruce (1996)
J. Biol. Chem. 271, 32907-32915
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Modulation of folding pathways of exported proteins by the leader sequence.
S Park, G Liu, T. Topping, W. Cover, and L. Randall (1988)
Science 239, 1033-1035
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Functional Signal Peptides Bind a Soluble N-terminal Fragment of SecA and Inhibit Its ATPase Activity.
T. L. Triplett, A. R. Sgrignoli, F.-B. Gao, Y.-B. Yang, P. C. Tai, and L. M. Gierasch (2001)
J. Biol. Chem. 276, 19648-19655
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