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Phospholipid flipping in biogenic membranes is a keyfeature of membrane bilayer assembly. Flipping is facilitated by proteinaceoustransporters (flippases) that do not need metabolic energy to function. Noflippase has yet been identified. The architecture of the E. coli proteintranslocon suggests that it could account for the flippase activity in thebacterial inner membrane. To test this possibility, we used E. coli cellsdepleted of SecYE or YidC to assay flipping in proteoliposomes reconstitutedfrom detergent extracts of their inner membranes. We conclude that the proteintranslocon contributes minimally, if at all, to phospholipid flippase activityin the inner membrane.

Reconstitution of Phospholipid Flippase Activity from E. coli Inner Membrane: A Test of the Protein Translocon as a Candidate Flippase