1. Identification of a protein at the ribosomal donor-site by affinity labeling
- Author
-
R. Hauptmann, Georg Stöffler, Ernst Kuechler, H.O. Voorma, and A.P. Czernilofsky
- Subjects
Formates ,Receptors, Drug ,Biophysics ,Biology ,Sulfur Radioisotopes ,Biochemistry ,Ribosome ,Chromatography, Affinity ,Methionine ,Bacterial Proteins ,RNA, Transfer ,Peptide Initiation Factors ,Eukaryotic initiation factor ,Centrifugation, Density Gradient ,Escherichia coli ,Initiation factor ,Eukaryotic Small Ribosomal Subunit ,Peptide Chain Initiation, Translational ,Molecular Biology ,Immunoelectrophoresis ,Affinity labeling ,Eukaryotic Large Ribosomal Subunit ,Cell Biology ,Ribosomal RNA ,Electrophoresis, Polyacrylamide Gel ,Eukaryotic Ribosome ,Ribosomes - Abstract
p-nitrophenylcarbamyl-methionyl-tRNAfMet is shown to act as an analogue of fMet-tRNAfMet in initiation complex formation. It binds to E. coli ribosomes in the presence of initiation factors and R 17-RNA as messenger. Covalent bond formation occurs in the complex between the Met-tRNAfMet derivative and protein of the 50 S ribosomal subunit. The protein labeled predominantly in the reaction has been identified as L 27 indicating that this protein is located at the donor-site of the ribosome.
- Published
- 1974