Ribozyme-catalyzed tRNA aminoacylation

  title={Ribozyme-catalyzed tRNA aminoacylation},
  author={N Lee and Yoshitaka Bessho and Kenneth Wei and Jack W. Szostak and Hiroaki Suga},
  journal={Nature Structural Biology},
The RNA world hypothesis implies that coded protein synthesis evolved from a set of ribozyme catalyzed acyl-transfer reactions, including those of aminoacyl-tRNA synthetase ribozymes. We report here that a bifunctional ribozyme generated by directed in vitro evolution can specifically recognize an activated glutaminyl ester and aminoacylate a targeted tRNA, via a covalent aminoacyl-ribozyme intermediate. The ribozyme consists of two distinct catalytic domains; one domain recognizes the… 

Structural basis of specific tRNA aminoacylation by a small in vitro selected ribozyme

A comparison of two crystallographically independent flexizyme conformations suggests that this ribozyme may achieve enhanced specificity by coupling active-site folding to tRNA docking, reminiscent of the mutually induced fit of tRNA and protein employed by some aminoacyl-tRNA synthetases to increase specificity.

A tRNA aminoacylation system for non-natural amino acids based on a programmable ribozyme

It is shown that an in vitro–evolved ribozyme can also discriminate between specific tRNAs, and can transfer amino acids to the 3′ ends of cognate tRN as well as the CCA-3′ terminus and the anticodon loop of tRNAfMet.

An aminoacylation ribozyme evolved from a natural tRNA-sensing T-box riboswitch

A ribozyme is developed, Tx2.1, that is capable of aminoacylating tRNA with specificity for the anticodon from directed evolution of a T-box riboswitch, and could be used to charge non-natural amino acids in an in vitro translation system.

RNA Aminoacylation Mediated by Sequential Action of Two Ribozymes and a Nonactivated Amino Acid

This work presents two ribozymes connected by intermolecular base pairing and carrying out the two steps of aminoacylation: ribozyme 1 loads nonactivated phenylalanine onto its phosphorylated 5′ terminus, thereby forming a high‐energy mixed anhydride.

Flexizymes: their evolutionary history and the origin of catalytic function.

The history and development of these flexizymes and their appropriate substrates are described, which provide a versatile and easy-to-use tRNA acylation system.

An in vitro evolved precursor tRNA with aminoacylation activity

A set of catalysts for aminoacyl‐tRNA synthesis is an essential component for translation. The RNA world hypothesis postulates that RNA catalysts could have played this role. Here we show an in vitro

A view into the origin of life: aminoacyl-tRNA synthetases

The current understanding of the origin and evolution of aminoacyl-tRNA synthetases is reviewed, and the implications of these studies on the origin of life are discussed.

Catalyzed and spontaneous reactions on ribozyme ribose.

It is shown that a five-nucleotide RNA enzyme, reacting with a tetranucleotide substrate and elevated PheAMP, forms aminoacyl- and peptidyl-RNAs RNA-Phe through RNA- Phe(5), which comprises a true RNA enzyme.

Peptidyltransfer Reaction Catalyzed by the Ribosome and the Ribozyme: a Dissertation

The newly established assay for ribosomal peptidyltransferase reaction provides a good system to investigate the mechanism of ribosome reaction and may have potential application in drug screening to search for the specific peptidoltransferase inhibitors.



A novel ribozyme with ester transferase activity.

Peptide bond formation by in vitro selected ribozymes

This work demonstrates the in vitro selection of ribozymes (196 nucleotides) that perform the same peptidyl transferase reaction as the ribosome: that is, they can join amino acids by a peptide bond.

Ribozyme-catalysed amino-acid transfer reactions

In vitro selection and evolution is used to isolate ribozymes with acyl transferase activity from a pool of random RNA sequences and one of them transfers an amino acid to itself in a reaction that is analogous to peptidyl transfer on the ribosome.

Structural and kinetic characterization of an acyl transferase ribozyme.

Competitive inhibition experiments with unacylated substrate oligonucleotide are consistent with the ribozyme acting to stabilize substrate binding to the template, while negative interactions with the aminoacyl portion of the substrate destabilize binding.

An operational RNA code for amino acids and possible relationship to genetic code.

Members of the two different classes of tRNA synthetases are, like tRNAs, organized into two major domains, and the emergence of the genetic from the operational RNA code could occur when the second domain of synthetase was added with the anticodon-containing domain of t RNAs.

Aminoacyl esterase activity of the Tetrahymena ribozyme.

The ability of RNA to catalyze reactions with aminoacyl esters expands the catalytic versatility of RNA and suggests that the first aminoacyL tRNA synthetase could have been an RNA molecule.

Rules that govern tRNA identity in protein synthesis.

  • W. McClain
  • Biology, Chemistry
    Journal of molecular biology
  • 1993
The specificity of tRNA in protein synthesis depends not only on its recognition of the codon in the mRNA, but also on its Recognition of the correct aminoacyl-tRNA synthetase enzyme, which ensures both productive and non-productive interactions with the respective enzymes.

Essential structures of a self-aminoacylating RNA.

It appears that a complex RNA active center can be assembled by specifying unexpectedly few nucleotides, perhaps with a critical contribution from an essential calcium ion.

A specific amino acid binding site composed of RNA.

The arginine site can be placed within the G site by structural homology, with consequent implications for RNA-amino acid interaction, for the origin of the genetic code, for control of RNA activities, and for further catalytic capabilities for RNA.

Selection of RNA amide synthases.