par Demel, R A;Goormaghtigh, Erik ;de Kruijff, B
Référence Biochimica et biophysica acta, 1027, 2, page (155-162)
Publication Publié, 1990-08
Article révisé par les pairs
Résumé : The present data show the critical importance of the anionic lipid content in monomolecular layers for the interaction with PhoE signal peptide. At 37 degrees C and 100 mM NaCl the interaction is maximal at 30-40 mol% anionic lipid. The results correlate with the reduced translocation competence of Escherichia coli strain HD3122, which has a much lower anionic lipid content as compared to the wild-type strain SD12 (De Vrije et al. (1988) Nature 334, 173-175). PhoE signal peptide analogs as N-formyl PhoE signal peptide, PhoE signal peptide +(1-7) and PhoE signal peptide Val-8----Trp-8 show the same lipid preference as PhoE signal peptide. On the other hand the affinity for an anionic lipid interface is strongly reduced for PhoE signal peptide Lys-19,-20----Asp-19,-20, which correlates with the less efficient translocation of PhoE protein carrying this signal sequence. At limiting anionic lipid concentrations there is a temperature and salt effect on the observed interaction, which is related to a conformational change of the peptide. Signal sequences show clearly conformational flexibility in responds to environmental conditions. Under the conditions used in this study FTIR spectra of PhoE signal peptide-DOPG monolayers show a high content of beta-structure and beta-turn.