Journal of Molecular Biology · 2013 · 30 citations · 22 references
Life SciencesBiochemistryMicrobiologyMembrane BiochemistryMembrane BiophysicsMolecular BiophysicsBiological MembranesMembrane Protein TopologyMembrane ProteinsMembrane TransportSecretory PathwayTransport Across Biological MembranesAlpha HelicesCo-translational Membrane InsertionEscherichia ColiProtein Insertion Into MembranesProtein Translocation Into The Endoplasmic ReticulumSec61 ComplexTransmembrane HelicesTransmembrane Proteins
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.
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Recognition of transmembrane helices by the endoplasmic reticulum translocon
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Molecular code for transmembrane-helix recognition by the Sec61 translocon
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YidC mediates membrane protein insertion in bacteria
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