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lüll Helix insertion into bilayers and the evolution of membrane proteins Renthal RCell Mol Life Sci 2010[Apr]; 67 (7): 1077-88Polytopic alpha-helical membrane proteins cannot spontaneously insert into lipid bilayers without assistance from polytopic alpha-helical membrane proteins that already reside in the membrane. This raises the question of how these proteins evolved. Our current knowledge of the insertion of alpha-helices into natural and model membranes is reviewed with the goal of gaining insight into the evolution of membrane proteins. Topics include: translocon-dependent membrane protein insertion, antibiotic peptides and proteins, in vitro insertion of membrane proteins, chaperone-mediated insertion of transmembrane helices, and C-terminal tail-anchored (TA) proteins. Analysis of the E. coli genome reveals several predicted C-terminal TA proteins that may be descendents of proteins involved in pre-cellular membrane protein insertion. Mechanisms of pre-translocon polytopic alpha-helical membrane protein insertion are discussed.|Amino Acid Sequence[MESH]|Bacteriocins/metabolism[MESH]|Calcium-Binding Proteins/metabolism[MESH]|Cell Membrane/chemistry/*metabolism[MESH]|Evolution, Molecular[MESH]|Lipid Bilayers/chemistry/metabolism[MESH]|Membrane Glycoproteins/metabolism[MESH]|Membrane Proteins/*chemistry/metabolism[MESH]|Molecular Chaperones/metabolism[MESH]|Molecular Sequence Data[MESH]|Protein Structure, Secondary[MESH]|Receptors, Cytoplasmic and Nuclear/metabolism[MESH]|Receptors, Peptide/metabolism[MESH] |