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Conformations of Signal Peptides Induced by Lipids Suggest Initial Steps in Protein Export
Martha S. Briggs, Donald G. Cornell, Richard A. Dluhy and Lila M. Gierasch
New Series, Vol. 233, No. 4760 (Jul. 11, 1986), pp. 206-208
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/1697187
Page Count: 3
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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 λ 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 α-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 β structure. These observations are combined in a model for the initial steps in signal sequence-membrane interaction in vivo.
Science © 1986 American Association for the Advancement of Science