A vocabulary of ancient peptides at the origin of folded proteins

Elife. 2015 Dec 14:4:e09410. doi: 10.7554/eLife.09410.

Abstract

The seemingly limitless diversity of proteins in nature arose from only a few thousand domain prototypes, but the origin of these themselves has remained unclear. We are pursuing the hypothesis that they arose by fusion and accretion from an ancestral set of peptides active as co-factors in RNA-dependent replication and catalysis. Should this be true, contemporary domains may still contain vestiges of such peptides, which could be reconstructed by a comparative approach in the same way in which ancient vocabularies have been reconstructed by the comparative study of modern languages. To test this, we compared domains representative of known folds and identified 40 fragments whose similarity is indicative of common descent, yet which occur in domains currently not thought to be homologous. These fragments are widespread in the most ancient folds and enriched for iron-sulfur- and nucleic acid-binding. We propose that they represent the observable remnants of a primordial RNA-peptide world.

Keywords: LUCA; RNA-peptide world; ancient peptides; biochemistry; biophysics; domain evolution; none; protein evolution; structural biology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology
  • Evolution, Molecular*
  • Genetic Variation*
  • Protein Folding*
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Proteins / genetics*

Substances

  • Proteins

Grants and funding

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.