Dimer state of protein L7/L12 and EF-G-dependent reactions of ribosomes.
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.
D004926:Escherichia coli / Q000378:metabolism*; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000378:metabolism; D046911:Macromolecular Substances; D008970:Molecular Weight; D010441:Peptide Chain Elongation, Translational; D010445:Peptide Elongation Factors / Q000378:metabolism*; D014176:Protein Biosynthesis; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D046911:Macromolecular Substances; D010445:Peptide Elongation Factors; D012269:Ribosomal Proteins; D006153:Guanosine Diphosphate; D020963:GTP Phosphohydrolase-Linked Elongation Factors