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PMID: 4567331 Published · ppublish English Journal Article

Identity of the ribosomal proteins involved in the interaction with elongation factor G.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 70 ·No. 1 ·1973-01-00 ·Pages 147-50

Highland JH, Bodley JW, Gordon J, Hasenbank R, Stöffler G

Abstract

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.

MeSH Terms
Animals Antigen-Antibody Complex Antigens/analysis Escherichia coli/analysis Guanine Nucleotides/metabolism Immunoassay Immunoglobulin G Peptide Elongation Factors Proteins/analysis,isolation & purification,metabolism Rabbits/immunology Ribosomes/analysis,immunology,metabolism Structure-Activity Relationship Tritium
Chemicals
Antigen-Antibody Complex Antigens Guanine Nucleotides Immunoglobulin G Peptide Elongation Factors Proteins Tritium
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Highland J H
Bodley J W
Gordon J
Hasenbank R
Stöffler G
References (28)
28 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.70.1.147
Published
1973-01-00
Pages
147-50
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433203
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.70.1.147 PMC Full Text View journal details
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