Title
A selected ribozyme catalyzing diverse dipeptide synthesis
Academic Program
Not applicable
UMMS Affiliation
Graduate School of Biomedical Sciences; Program in Molecular Medicine
Publication Date
2002-05-29
Document Type
Article
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
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
10.1016/S1074-5521(02)00141-2
Source
Chem Biol. 2002 May;9(5):619-28.
Journal/Book/Conference Title
Chemistry and biology
Related Resources
PubMed ID
12031668
Repository Citation
Sun L, Cui Z, Gottlieb RL, Zhang B. (2002). A selected ribozyme catalyzing diverse dipeptide synthesis. GSBS Student Publications. https://doi.org/10.1016/S1074-5521(02)00141-2. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/1214