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PMID: 361401 Published · ppublish English Journal Article

Dimer state of protein L7/L12 and EF-G-dependent reactions of ribosomes.

European journal of biochemistry ·Vol. 90 ·No. 2 ·1978-10-00 ·Pages 319-23

Koteliansky VE, Domogatsky SP, Gudkov AT

Abstract

A number of different monomer and dimer derivatives of protein L7/L12 has been studied in EF-G-dependent reactions on the ribosome. It has been shown that only dimer derivatives of protein L7/L12 are able to interact with the ribosome. This means that it is the dimer forms of protein L7/L12 that are present in the functionally active ribosome. It is likely that the N-terminal sequence of protein L7/L12 is responsible for dimerization of the protein in solution and at the same time contributes mainly to the interaction of the protein L7/L12 dimer with the ribosome. The results obtained suggest that there are four copies of protein L7/L12 in the translating ribosome.

MeSH Terms
Escherichia coli/metabolism GTP Phosphohydrolase-Linked Elongation Factors/metabolism Guanosine Diphosphate/metabolism Macromolecular Substances Molecular Weight Peptide Chain Elongation, Translational Peptide Elongation Factors/metabolism Protein Biosynthesis Ribosomal Proteins/metabolism Ribosomes/metabolism
Chemicals
Macromolecular Substances Peptide Elongation Factors Ribosomal Proteins Guanosine Diphosphate GTP Phosphohydrolase-Linked Elongation Factors
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Koteliansky V E
Domogatsky S P
Gudkov A T
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1978-10-00
Pages
319-23
Language
English
Region
England
NLM ID
0107600
Subset
IM
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