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Evolution of outer membrane beta-barrels from an ancestral beta beta hairpin.

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Soeding,  J.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Remmert, M., Biegert, A., Linke, D., Lupas, A. N., & Soeding, J. (2010). Evolution of outer membrane beta-barrels from an ancestral beta beta hairpin. Molecular Biology and Evolution, 27(6), 1348-1358. doi:10.1093/molbev/msq017.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0017-9693-6
Abstract
Outer membrane β-barrels (OMBBs) are the major class of outer membrane proteins from Gram-negative bacteria, mitochondria, and plastids. Their transmembrane domains consist of 8–24 β-strands forming a closed, barrel-shaped β-sheet around a central pore. Despite their obvious structural regularity, evidence for an origin by duplication or for a common ancestry has not been found. We use three complementary approaches to show that all OMBBs from Gram-negative bacteria evolved from a single, ancestral ββ hairpin. First, we link almost all families of known single-chain bacterial OMBBs with each other through transitive profile searches. Second, we identify a clear repeat signature in the sequences of many OMBBs in which the repeating sequence unit coincides with the structural ββ hairpin repeat. Third, we show that the observed sequence similarity between OMBB hairpins cannot be explained by structural or membrane constraints on their sequences. The third approach addresses a longstanding problem in protein evolution: how to distinguish between a very remotely homologous relationship and the opposing scenario of “sequence convergence.” The origin of a diverse group of proteins from a single hairpin module supports the hypothesis that, around the time of transition from the RNA to the protein world, proteins arose by amplification and recombination of short peptide modules that had previously evolved as cofactors of RNAs.