4.5 Article

Single-molecule paleoenzymology probes the chemistry of resurrected enzymes

Journal

NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 5, Pages 592-U99

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2020

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Funding

  1. US National Institutes of Health [HL061228, HL066030]
  2. Spanish Ministry of Science and Innovation
  3. NASA Astrobiology (Georgia Institute of Technology)
  4. NASA Exobiology
  5. Fundacion Ibercaja and Fundacion Caja Madrid
  6. Fundacion Alfonso Martin Escudero

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It is possible to travel back in time at the molecular level by reconstructing proteins from extinct organisms. Here we report the reconstruction, based on sequence predicted by phylogenetic analysis, of seven Precambrian thioredoxin enzymes (Trx) dating back between similar to 1.4 and similar to 4 billion years (Gyr). The reconstructed enzymes are up to 32 degrees C more stable than modern enzymes, and the oldest show markedly higher activity than extant ones at pH 5. We probed the mechanisms of reduction of these enzymes using single-molecule force spectroscopy. From the force dependency of the rate of reduction of an engineered substrate, we conclude that ancient Trxs use chemical mechanisms of reduction similar to those of modern enzymes. Although Trx enzymes have maintained their reductase chemistry unchanged, they have adapted over 4 Gyr to the changes in temperature and ocean acidity that characterize the evolution of the global environment from ancient to modern Earth.

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