Playing RNase P Evolution: Swapping the RNA Catalyst for a Protein Reveals Functional Uniformity of Highly Divergent Enzyme Forms

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Many biocatalysts apparently evolved independently more than once, leading to structurally unrelated macromolecules catalyzing the same biochemical reaction. The RNase P enzyme family is an exceptional case of this phenomenon called convergent evolution. RNase P enzymes use not only unrelated, but chemically distinct macromolecules, either RNA or protein, to catalyze a specific step in the biogenesis of transfer RNAs, the ubiquitous adaptor molecules in protein synthesis. However, this fundamental difference in the identity of the actual catalyst, together with a broad variation in structural complexity of the diverse forms of RNase P, cast doubts on their functional equivalence. Here we compared two of the structurally most extreme variants of RNase P by replacing the yeast nuclear enzyme, a 10-subunit RNA-protein complex, with a single-protein from plants representing the apparently simplest form of RNase P. Surprisingly, the viability and fitness of these RNase P-swapped yeasts and their molecular analyses demonstrated the full functional exchangeability of the highly dissimilar enzymes. The RNase P family, with its combination of structural diversity and functional uniformity, thus not only truly represents an extraordinary case of convergent evolution, but also demonstrates that increased structural complexity does not necessarily entail broadened functionality, but may rather be the result of “neutral” evolutionary mechanisms.

Vyšlo v časopise: Playing RNase P Evolution: Swapping the RNA Catalyst for a Protein Reveals Functional Uniformity of Highly Divergent Enzyme Forms. PLoS Genet 10(8): e32767. doi:10.1371/journal.pgen.1004506
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1004506

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