Title of article :
Quantitative Analysis of SecYEG-Mediated Insertion of Transmembrane α-Helices into the Bacterial Inner Membrane
Author/Authors :
Karin ?jemalm، نويسنده , , Salomé Calado Botelho، نويسنده , , Chiara Stüdle، نويسنده , , Gunnar von Heijne، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2013
Abstract :
Most integral membrane proteins, both in prokaryotic and eukaryotic cells, are co-translationally inserted into the membrane via Sec-type translocons: the SecYEG complex in prokaryotes and the Sec61 complex in eukaryotes. The contributions of individual amino acids to the overall free energy of membrane insertion of single transmembrane α-helices have been measured for Sec61-mediated insertion into the endoplasmic reticulum (ER) membrane (Nature 450:1026–1030) but have not been systematically determined for SecYEG-mediated insertion into the bacterial inner membrane. We now report such measurements, carried out in Escherichia coli. Overall, there is a good correlation between the results found for the mammalian ER and the E. coli inner membrane, but the hydrophobicity threshold for SecYEG-mediated insertion is distinctly lower than that for Sec61-mediated insertion.
Keywords :
leader peptidase , transmembrane helix , SecYEG , membrane protein
Journal title :
Journal of Molecular Biology
Journal title :
Journal of Molecular Biology