<p>A recent study by Liam Longo and co-workers at the Earth-Life Science Institute, published in Angewandte Chemie, reports the discovery of an ancient helix-hairpin-helix protein motif capable of functioning in both left- and right-handed forms, thus challenging the concept that biomolecular interactions are strictly dependent on homochirality. This rather rare “ambidextrous” property suggests that such motifs may be molecular relics from a pre-LUCA era when mirror-image life forms coexisted, and offers new insights into the origins and evolution of molecular asymmetry seen in living matter.</p> Graphical abstract <p>The ‘helix-hairpin-helix’ motif allows the binding of a simple peptide to both DNA and its mirror image. Credit: Liam M S Longo.</p>

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Ancient ambidextrous protein defies the rule of molecular handedness

  • Dibyendu Das

摘要

A recent study by Liam Longo and co-workers at the Earth-Life Science Institute, published in Angewandte Chemie, reports the discovery of an ancient helix-hairpin-helix protein motif capable of functioning in both left- and right-handed forms, thus challenging the concept that biomolecular interactions are strictly dependent on homochirality. This rather rare “ambidextrous” property suggests that such motifs may be molecular relics from a pre-LUCA era when mirror-image life forms coexisted, and offers new insights into the origins and evolution of molecular asymmetry seen in living matter.

Graphical abstract

The ‘helix-hairpin-helix’ motif allows the binding of a simple peptide to both DNA and its mirror image. Credit: Liam M S Longo.