Ribozyme-catalysed amino-acid transfer reactions
- 30 May 1996
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 381 (6581) , 442-444
- https://doi.org/10.1038/381442a0
Abstract
THE 'RNA world' hypothesis proposes an early stage in the evolution of life in which both genomic and catalytic functions were fulfilled by RNA1. The evolution of RNA-catalysed protein synthesis would have been a necessary step in the transition from such an RNA world to modern protein-dominated biology. For this to have been possible, RNA must be capable of catalysing amide-bond formation using acylated carrier RNA substrates as amino-acid donors. We have used in vitro selection and evolution to isolate ribozymes with acyl transferase activity from a pool of random RNA sequences. One of these acyl transferases with a 5′-amino group transfers an amino acid to itself in a reaction that we propose to be analogous to peptidyl transfer on the ribosome.Keywords
This publication has 10 references indexed in Scilit:
- In vitro evolution of a self-alkylatlng ribozymeNature, 1995
- Isolation of New Ribozymes from a Large Pool of Random SequencesScience, 1993
- Randomization of genes by PCR mutagenesis.Genome Research, 1992
- Unusual Resistance of Peptidyl Transferase to Protein Extraction ProceduresScience, 1992
- DNA trapping electrophoresisNature, 1990
- Studies on the catalytic rate constant of ribosomal peptidyltransferaseBiochimica et Biophysica Acta (BBA) - General Subjects, 1987
- Origin of life: The RNA worldNature, 1986
- Characterization of the branch site in lariat RNAs produced by splicing of mRNA precursorsNature, 1985
- Template catalysis of acetyl transfer reactionsBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971
- Ribosome-catalyzed ester formationBiochemistry, 1970