RESUMO
Most proteins destined for secretion are synthesized with amino-terminal extensions, known as signal peptides, which play a vital role in their translocation across the membrane bordering the cytoplasm. Following translocation across the eukaryotic endoplasmic reticulum (ER) membrane or the bacterial cytoplasmic membrane, signal peptides are proteolytically removed from the preproteins. The process of membrane protein assembly can be likened to that of protein export in that it involves the translocation of portions of proteins across membranes. Moreover, the topological similarities between eukaryotic ER and plasma membrane proteins and bacterial cytoplasmic membrane proteins suggest that the mechanisms of membrane protein assembly may, like those of protein export, share fundamental similarities in eukaryotic and bacterial cells. However, whilst many of the ER and plasma membrane proteins of higher eukaryotes are synthesized with cleavable signal peptides, the same is true of only very few bacterial cytoplasmic membrane proteins. This fact is not widely appreciated, probably because certain exceptional (signal peptide-containing) bacterial membrane proteins, such as the major coat protein of bacteriophage M13, have been the subject of extensive investigations. In this review we highlight this anomaly and discuss it within the general context of membrane protein topology.
