Amino acids as RNA ligands: a direct-RNA-template theory for the code's origin.
Numerous RNA binding sites for specific amino acids are now known, coming predominantly from selection-amplification experiments. These sites are chemically discriminating despite being predominantly small, simple RNA structures: internal and bulge loops. Recent studies of sites for hydrophobic side chains suggest that there are other generalizable structural features which recur in hydrophobic RNA sites. Further, sites for hydrophobic side chains can contain codons for the bound amino acid, as has also long been known for the polar amino acid arginine. Such findings are comprehensively reviewed, and the implications for the origin of coded peptide synthesis are considered. An origins hypothesis which accommodates all the data, DRT (direct RNA templating), is formulated.
Yarus
M
M
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309-0347, USA. yarus@stripe.colorado.edu
D000596:Amino Acids / Q000378:metabolism*; D001120:Arginine / Q000235:genetics; D001665:Binding Sites; D019143:Evolution, Molecular; D005815:Genetic Code; D008024:Ligands; D008957:Models, Genetic; D009690:Nucleic Acid Conformation; D010452:Peptide Biosynthesis / Q000235:genetics; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D016053:RNA, Protozoan / Q000235:genetics
D000596:Amino Acids; D008024:Ligands; D016053:RNA, Protozoan; D012313:RNA; D001120:Arginine