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…
4 Citations
Identification of proteins at the peptidyl-tRNA binding site of rat liver ribosomes
- Biology, ChemistryMolecular and General Genetics MGG
- 2004
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.
Beyond the survival and death of the deltamethrin-threatened pollen beetle Meligethes aeneus: An in-depth proteomic study employing a transcriptome database.
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Affinity labelling of yeast ribosomal peptidyl transferase
- Biology, ChemistryMolecular and General Genetics MGG
- 2004
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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