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Identity of the Ribosomal Proteins Involved in the Interaction with Elongation Factor G

Rabbit antibodies produced against 50 of the 55 individually purified ribosomal proteins of Escherichia coli were tested for their ability to interfere with the formation of the ribosome· EF-G· GDP complex. Only antibodies produced against proteins L7 and L12 inhibited complex formation, and they di...

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Published in:	Proceedings of the National Academy of Sciences - PNAS 1973-01, Vol.70 (1), p.147-150
Main Authors:	Highland, Joseph H., Bodley, James W., Gordon, Julian, Hasenbank, Renate, Stoffler, Georg
Format:	Article
Language:	English
Subjects:	Animals Antibodies Antigen-Antibody Complex Antigens - analysis Biochemistry Biological Sciences: Biochemistry Escherichia coli - analysis Guanine Nucleotides - metabolism Highlands Hydrolysis Immunoassay Immunoglobulin G Peptide Elongation Factors Protein synthesis Proteins Proteins - analysis Proteins - isolation & purification Proteins - metabolism Rabbits - immunology Ribosomal proteins Ribosomes Ribosomes - analysis Ribosomes - immunology Ribosomes - metabolism Structure-Activity Relationship Tritium
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cited_by	cdi_FETCH-LOGICAL-c3667-8116ef579ef43841434d14e6d885476081956ab4be897070f43cc9664c0b95c33
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container_issue	1
container_start_page	147
container_title	Proceedings of the National Academy of Sciences - PNAS
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creator	Highland, Joseph H. Bodley, James W. Gordon, Julian Hasenbank, Renate Stoffler, Georg
description	Rabbit antibodies produced against 50 of the 55 individually purified ribosomal proteins of Escherichia coli were tested for their ability to interfere with the formation of the ribosome· EF-G· GDP complex. Only antibodies produced against proteins L7 and L12 inhibited complex formation, and they did so completely. These two proteins were previously shown to be immunologically indistinguishable and necessary for the interaction between ribosomes and EF-G. The present data are consistent with the view that the interaction between ribosomes and EF-G that results in GTP hydrolysis occurs on, and is limited to, proteins L7 and L12 on the surface of the 50S ribosomal subunit.
doi_str_mv	10.1073/pnas.70.1.147
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source	PubMed Central Free; JSTOR Archival Journals and Primary Sources Collection
subjects	Animals Antibodies Antigen-Antibody Complex Antigens - analysis Biochemistry Biological Sciences: Biochemistry Escherichia coli - analysis Guanine Nucleotides - metabolism Highlands Hydrolysis Immunoassay Immunoglobulin G Peptide Elongation Factors Protein synthesis Proteins Proteins - analysis Proteins - isolation & purification Proteins - metabolism Rabbits - immunology Ribosomal proteins Ribosomes Ribosomes - analysis Ribosomes - immunology Ribosomes - metabolism Structure-Activity Relationship Tritium
title	Identity of the Ribosomal Proteins Involved in the Interaction with Elongation Factor G
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