Identification of the tRNA-binding sites on rat liver ribosomes by affinity labeling

@article{Czernilofsky2004IdentificationOT,
  title={Identification of the tRNA-binding sites on rat liver ribosomes by affinity labeling},
  author={A. P. Czernilofsky and Ekkehard Collatz and Axel M. Gressner and Ira G. Wool and Ernst K{\"u}chler},
  journal={Molecular and General Genetics MGG},
  year={2004},
  volume={153},
  pages={231-235}
}
Summaryp-Nitrophenoxycarbonyl-3H-phenylalanyl-tRNAyeastPhebinds to 80S rat liver ribosomes and forms a covalent bond with ribosomal proteins. The affinity labeled proteins were identified by a kind of “three-dimensional” electrophoresis: groups of 80S proteins were cut out of two-dimensional gel slabs, eluted, and separated by electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate; finally, the radioactivity in the protein bands was determined. The proteins L32/L33, L36, L21… 

Identification of proteins at the peptidyl-tRNA binding site of rat liver ribosomes

A model for the arrangement of proteins within this active site of rat liver peptidyl-tRNA is constructed, using a 3′-terminal pentanucleotide fragment of N-acetylleucyl-t RNA in which mercury atoms have been added at the C-5 position of the three cytosine residues.

Affinity labelling of yeast ribosomal peptidyl transferase

When only the components of the ribosomal P-site were analysed by reacting the treated particles with puromycin fewer spots were labelled, corresponding to proteins L36 and L19/20 using PNPC-Phe-tRNA and proteins L4/6, L36, and L43 using N-Iodoacetyl-P he-t RNA.

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