The TIM Barrel Architecture Facilitated the Early Evolution of Protein-Mediated Metabolism

• DOI: 10.1007/s00239-015-9722-8
• Publication Date: 2016-01-05T08:54:29Z
• Authors: Aaron David Goldman; Joshua T. Beatty; Laura F. Landweber
• Keywords: Proteome; Functional Diversity; Convergent evolution; Triosephosphate isomerase

The triosephosphate isomerase (TIM) barrel protein fold is a structurally repetitive architecture that present in approximately 10 % of all enzymes. It generally assumed this ubiquity modern proteomes reflects an essential historical role early protein-mediated metabolism. Here, we provide quantitative and comparative analyses to support several hypotheses about the importance TIM architecture. An information theoretical analysis structures supports hypothesis could arise more easily by duplication recombination compared other mixed α/β structures. We show enzymes corresponding most taxonomically broad superfamilies also have broadest range functions, often aided metal nucleotide-derived cofactors are thought reflect earlier stage metabolic evolution. By comparison putatively ancient architectures, find functional diversity proteins cannot be explained simply their antiquity. Instead, breadth functions can explained, part, incorporation cofactors, trend does not appear shared general. These results simple functionally general may arisen evolution biosynthesis provided ideal scaffold facilitate transition from ribozymes, peptides, geochemical catalysts