Peptide bond formation at the peptidyl transferase center on the ribosome is a crucial phenomenon in life systems. In this study, we conceptually propose possible roles of the RNA tetraplex as a scaffold for two aminoacyl minihelices that enable peptide bond formation. The basic rationale of this model is that "parallel" complementary templates composed of only 10-mer nucleotides can position two amino acids in close proximity, which is conceptually and essentially similar to the situation observed in ribosomes. Using supportive experimental data, we discuss the origin and evolution of peptide bond formation in early biological systems. © 2012 Elsevier Ireland Ltd.
Umehara, T., Kitagawa, T., Nakazawa, Y., Yoshino, H., Nemoto, R., & Tamura, K. (2012). RNA tetraplex as a primordial peptide synthesis scaffold. BioSystems, 109(2), 145–150. https://doi.org/10.1016/j.biosystems.2012.03.003