Quantitative analysis of SecYEG-mediated insertion of transmembrane α-helices into the bacterial inner membrane.
JSON
Ojemalm K, Botelho SC, Stüdle C, von Heijne G
J. Mol. Biol. 425 (15) 2813-2822 [2013-08-09; online 2013-05-07]
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.
PubMed 23659793
DOI 10.1016/j.jmb.2013.04.025
Crossref 10.1016/j.jmb.2013.04.025
pii: S0022-2836(13)00273-8