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Bacterial outer membrane proteins (OMPs) contain a unique “β barrel” segment that is inserted into the membrane by the  b arrel  a ssembly  m achinery (Bam) complex by an unknown mechanism. OMP assembly has been reconstituted  in vitro , but assembly reactions have involved the use of urea-denatured protein purified from inclusion bodies. Here we show that the  E. coli  Bam complex catalyzes the efficient assembly of OMPs synthesized de novo in a coupled  in vitro  transcription/translation system. Interestingly, the  in vitro  translated forms of the OMPs we analyzed were assembled more rapidly and were effectively engaged by fewer periplasmic chaperones than their urea-denatured counterparts. Taken together, our results strongly suggest that the mode of production influences the conformational states sampled by OMPs and thereby affects their recognition by both chaperones and the Bam complex. Besides providing insights into OMP biogenesis, our work describes a novel, streamlined method to reconstitute OMP assembly  in vitro .

Bam complex-mediated assembly of bacterial outer membrane proteins synthesized in an in vitro translation system