Proteins at the tRNA Binding Sites of Escherichia coli Ribosomes

p - Nitrophenylcarbamyl - phenylalanyl-tRNA binds to ribosomes in response to poly(U) and reacts with ribosomal proteins via covalent bond formation. Ribosomal proteins of Escherichia coli were characterized by two-dimensional gel electrophoresis and by reaction with specific antibodies. The affinit...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1974-01, Vol.71 (1), p.230-234
Hauptverfasser:	Czernilofsky, Armin P., Collatz, Ekkehard E., Stoffler, Georg, Kuechler, Ernst
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antibodies Antigen-Antibody Complex Autoradiography Bacterial Proteins - analysis Bacterial Proteins - metabolism Binding sites Binding Sites - drug effects Biological Sciences: Biochemistry Carbamates Centrifugation, Density Gradient Electrophoresis, Polyacrylamide Gel Escherichia coli Escherichia coli - cytology Escherichia coli - metabolism Gels Immunoassay Immunoglobulins Molecular Weight Nitrophenols Phenylalanine Protein Binding Proteins Puromycin - pharmacology Rabbits - immunology Radioactive decay Ribosomal proteins Ribosomes Ribosomes - metabolism RNA, Transfer - metabolism Transfer RNA Tritium
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Zusammenfassung:	p - Nitrophenylcarbamyl - phenylalanyl-tRNA binds to ribosomes in response to poly(U) and reacts with ribosomal proteins via covalent bond formation. Ribosomal proteins of Escherichia coli were characterized by two-dimensional gel electrophoresis and by reaction with specific antibodies. The affinity label is shown to react with the 50S proteins L27, L15, L2, L16, and L14. We therefore conclude that these particular proteins are located at or near tRNA-binding sites within the 50S ribosomal subunit.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.71.1.230