Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

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
Science
New Series, Vol. 233, No. 4760 (Jul. 11, 1986), pp. 206-208
Stable URL: http://www.jstor.org/stable/1697187
Page Count: 3
  • More info
  • Cite this Item
Conformations of Signal Peptides Induced by Lipids Suggest Initial Steps in Protein Export
Preview not available

Abstract

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.

Page Thumbnails

  • Thumbnail: Page 
206
    206
  • Thumbnail: Page 
207
    207
  • Thumbnail: Page 
208
    208