Ribozyme-catalyzed tRNA aminoacylation

@article{Lee2000RibozymecatalyzedTA,
  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},
  year={2000},
  volume={7},
  pages={28-33}
}
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

TLDR
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

TLDR
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

TLDR
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

TLDR
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.

TLDR
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

TLDR
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.

TLDR
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

TLDR
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.
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