Singhal, Abhishek4; Bagnacani, Valentina3; Corradini, Roberto3; Nielsen, Peter E4
1 Section II. Building 18.2, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, Københavns Universitet2 RNA and Gene Medicine Program, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, Københavns Universitet3 unknown4 Section II. Building 18.2, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, Københavns Universitet
Peptide synthesis is a fundamental feature of life. However, it still remains unclear how the contemporary translation apparatus evolved from primitive prebiotic systems and at which stage of the evolution peptide synthesis emerged. Using simple molecular architectures, in which aminoacyl transfer of phenylalanine occurs either between two ends of a PNA stem loop structure, between two PNAs in a duplex, or between two PNAs assembled on a PNA template, we show that bona fide template instructed phenylalanine transfer can take place. Thus, we have identified conditions which allow template assisted intermolecular aminoacyl transfer using simple ester aminolysis chemistry primitively analogous to the ribosomal peptidyl transferase reaction in the absence of anchimeric assistance from ribose and ribosome catalysis. These results help define the minimum chemical boundary conditions for the translation process and also give insight into the possibilities for the prebiotic emergence of RNA-independent translation.
Acs Chemical Biology, 2014, Vol 9, Issue 11, p. 2612-2620