A selected ribozyme catalyzing diverse dipeptide synthesis

Academic Program

Not applicable

UMMS Affiliation

Graduate School of Biomedical Sciences; Program in Molecular Medicine

Publication Date


Document Type



Life Sciences | Medicine and Health Sciences


The sequence of events by which protein, RNA, and DNA emerged during early biological evolution is one of the most profound questions regarding the origin of life. The contemporary role of aminoacyl-adenylates as intermediates in both ribosomal and nonribosomal peptide synthesis suggests that they may have served as substrates for uncoded peptide synthesis during early evolution. We report a highly active peptidyl transferase ribozyme family, isolated by in vitro selection, that efficiently catalyzes dipeptide synthesis by using an aminoacyl-adenylate substrate. It was characterized by sequence and structural analysis and kinetic studies. Remarkably, the ribozyme catalyzed the formation of 30 different dipeptides, the majority of rates being within 5-fold that of the Met-Phe dipeptide required by the selection. The isolation of this synthetic ribozyme fosters speculation that ribozyme-mediated uncoded peptide synthesis may have preceded coded peptide synthesis.

DOI of Published Version



Chem Biol. 2002 May;9(5):619-28.

Journal/Book/Conference Title

Chemistry and biology

Related Resources

Link to Article in PubMed

PubMed ID