Prebiotic chiral transfer from self-aminoacylating ribozymes may favor either handedness

Josh Kenchel, Alberto Vázquez-Salazar, Reno Wells, Krishna Brunton, Evan Janzen, Kyle M. Schultz, Ziwei Liu, Weiwei Li, Eric T. Parker, Jason P. Dworkin and Irene A. Chen ()
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Josh Kenchel: University of California
Alberto Vázquez-Salazar: University of California
Reno Wells: University of California
Krishna Brunton: University of California
Evan Janzen: University of California
Kyle M. Schultz: University of California
Ziwei Liu: University of Cambridge
Weiwei Li: University of California
Eric T. Parker: NASA Goddard Space Flight Center
Jason P. Dworkin: NASA Goddard Space Flight Center
Irene A. Chen: University of California

Nature Communications, 2024, vol. 15, issue 1, 1-9

Abstract: Abstract Modern life is essentially homochiral, containing D-sugars in nucleic acid backbones and L-amino acids in proteins. Since coded proteins are theorized to have developed from a prebiotic RNA World, the homochirality of L-amino acids observed in all known life presumably resulted from chiral transfer from a homochiral D-RNA World. This transfer would have been mediated by aminoacyl-RNAs defining the genetic code. Previous work on aminoacyl transfer using tRNA mimics has suggested that aminoacylation using D-RNA may be inherently biased toward reactivity with L-amino acids, implying a deterministic path from a D-RNA World to L-proteins. Using a model system of self-aminoacylating D-ribozymes and epimerizable activated amino acid analogs, we test the chiral selectivity of 15 ribozymes derived from an exhaustive search of sequence space. All of the ribozymes exhibit detectable selectivity, and a substantial fraction react preferentially to produce the D-enantiomer of the product. Furthermore, chiral preference is conserved within sequence families. These results are consistent with the transfer of chiral information from RNA to proteins but do not support an intrinsic bias of D-RNA for L-amino acids. Different aminoacylation structures result in different directions of chiral selectivity, such that L-proteins need not emerge from a D-RNA World.

Date: 2024
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DOI: 10.1038/s41467-024-52362-x

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