Gram-negative outer-membrane proteins with multiple β-barrel domains

Outer-membrane beta barrels (OMBBs) are found in the outer membrane of gram-negative bacteria and eukaryotic organelles. OMBBs fold as antiparallel beta-sheets that close onto themselves, forming pores that traverse the membrane. Currently known structures include only one barrel, of 8 to 36 strands, per chain. The lack of multi-OMBB chains is surprising, as most OMBBs form oligomers, and some function only in this state. Using a combination of sensitive sequence comparison methods and coevolutionary analysis tools, we identify many proteins combining multiple beta barrels within a single chain; combinations that include eight-stranded barrels prevail. These multibarrels seem to be the result of independent, lineage-specific fusion and amplification events. The absence of multibarrels that are universally conserved in bacteria with an outer membrane, coupled with their frequent de novo genesis, suggests that their functions are not essential but rather beneficial in specific environments. Adjacent barrels of complementary function within the same chain may allow for functions beyond those of the individual barrels.

Automated summary

Research has identified many proteins combining multiple beta barrels within a single chain, with combinations that include eight-stranded barrels prevailing. These multibarrels seem to result from independent, lineage-specific fusion and amplification events. The absence of universally conserved multibarrels in bacteria with an outer membrane, along with their frequent de novo genesis, suggests that their functions are beneficial rather than essential in specific environments.