Passage of proteins across membranes during export from their site of synthesis to their final destination is mediated by leader peptides that paradoxically exhibit a unity of function in spite of a diversity of sequence. These leader peptides act in at least two stages of the export process: at entry into the pathway and subsequently during translocation across the membrane. How selectivity is imposed on the system in the absence of a consensus among the sequences of leader peptides is the main issue discussed here.
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