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Science 31 May 1985:
Vol. 228. no. 4703, pp. 1096 - 1099
DOI: 10.1126/science.3158076
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Articles

Science, Vol 228, Issue 4703, 1096-1099
Copyright © 1985 by American Association for the Advancement of Science

articles

In vivo function and membrane binding properties are correlated for Escherichia coli lamB signal peptides

MS Briggs, LM Gierasch, A Zlotnick, JD Lear, and WF DeGrado

Wild-type and pseudorevertant signal peptides of the lamB gene product of Escherichia coli interact with lipid systems whereas a nonfunctional deletion mutant signal peptide does not. This conclusion is based on interaction of synthetic signal peptides with a lipid monolayer-water surface, conformational changes induced by presence of lipid vesicles in an aqueous solution of signal peptide, and capacities of the peptides to promote vesicle aggregation. Analysis of the signal sequences and previous conformational studies suggest that these lipid interaction properties may be attributable to the tendency of the functional signal peptides to adopt alpha-helical conformations. Although the possibility of direct interaction between the signal peptide and membrane lipids during protein secretion is controversial, the results suggest that conformationally related amphiphilicity and consequent membrane affinity of signal sequences are important for function in vivo.


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Modulation of folding pathways of exported proteins by the leader sequence.
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Conformations of signal peptides induced by lipids suggest initial steps in protein export.
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