[Structural analysis of translating ribosomes. Proton magnetic resonance method].
Comparison has been made of the proton magnetic resonance (PMR) spectra of translating ribosomes in the pre-translocation and post-translocation states as well as of the complexes of translating ribosomes with elongation factors Tu (EF-Tu) or G (EF-G) in the presence of the uncleavable analogue of GTP--guanylyl-imidodiphosphate (GMP-PNP). It is shown that proteins L7/L12 within the translating ribosomes possess a high intramolecular mobility both in the pre-translocation and in the post-translocation states. The interaction of EF-G with translating ribosomes results in a decrease of the mobility of the L7/L12 proteins. The interaction of EF-Tu with translating ribosomes leads to slight changes in the PMR spectra different from the changes caused by EF-G.
Riabova
L A
LA
Okon
M S
MS
Bushuev
V N
VN
Baranov
V I
VI
D009682:Magnetic Resonance Spectroscopy; D020653:Peptide Elongation Factor G; D010444:Peptide Elongation Factor Tu / Q000032:analysis; D010445:Peptide Elongation Factors / Q000032:analysis; D014176:Protein Biosynthesis; D012269:Ribosomal Proteins / Q000032:analysis*; D012270:Ribosomes / Q000032:analysis*
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12; D010444:Peptide Elongation Factor Tu
Strukturnye issledovaniia transliruiushchikh ribosom. III. Metod protonnogo magnitnogo rezonansa.