Signal sequence-dependent assembly of Tat translocon subunits (P13)

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Transporting proteins across cellular membranes is a vital process. Most transported proteins pass in an unfolded conformation through proteinaceous structures (translocons). In contrast, the bacterial twin-arginine translocon (Tat) translocates fully folded proteins, some of which representing virulence factors. Without compromising the membrane barrier, the Tat translocon forms a transient conduit of unknown structure from four membrane proteins (TatA,B,C,E). By reconstituting the purified TatABCE proteins into transport-competent proteoliposomes and by employing measures to arrest the transport event, the composition of a functional Tat translocon will be elucidated.