Ribozyme-catalysed amino-acid transfer reactions

Article Abstract:

RNA sequences with acyl transferase activity containing a 5'-amino group are capable of transferring an amino acid to themselves. This reaction is similar to peptidyl transfer on ribosomes. RNA can accelerate the chemical reactions in protein synthesis. A ribozyme with 3'-OH to 3'-OH acyl-transferase activity was probably the precursor of rRNA. The results of the study agree with the RNA world hypothesis according to which RNA was responsible for both the catalytic and genomic function in the early stages of the evolution of life.

Analysis, Transferases

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Evolution ex vivo

Article Abstract:

Mutagenesis of the Tetrahymena ribozyme was studied using directed in vitro evolution. Niles Lehman and Gerald F. Joyce altered the ribozyme's metal ion specificity to determine the effect on production of mutant forms. Clones, derived from a 5% mutagenesis of a large number of mutants, were sequenced. Only 2.26 sequences produced beneficial mutations. An increase in gene pool activity generated a concomitant increase in number of mutations per sequence. The mutations did not affect the ribozyme's metal-binding site.

Genetic aspects, Evolution (Biology), Evolution, Mutagenesis

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In vitro evolution of a self-alkylating ribozyme

Article Abstract:

A specific ribozyme isolated from a group of random sequence RNAs is capable of binding to non-nucleic acid substrates and contains enzymes which can catalyze chemical reactions besides the normal phosphate-sugar reactions. The self-alkylating ribozyme shows the possibility that RNA provided both the genetically transferable information and enzymes required by the first formed cells.

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