[Mechanism of codon-anticodon interaction in ribosomes. Interaction of aminoacyl-tRNA with 70S ribosomes in the absence of elongation factor EF-Tu and GTP].
Purified Phe-tRNAPhe revealed higher affinity to the donor (D) site of vacant 70S . poly(U) complex than to the acceptor (A) site, independent on Mg2+ concentration. As a result, in excess of ribosomes Phe-tRNAPhe binds exclusively to the D site. This was proved using the tests in the presence of tetracycline and puromycin. Preferential binding of Phe-tRNAPhe to the D site was used to measure equilibrium association constants of this interaction at different temperatures and Mg2+ concentrations. A large value of reaction enthalpy (ca. -26 Kcal/mole) was found.
D000926:Anticodon / Q000235:genetics*; D001426:Bacterial Proteins / Q000378:metabolism; D002151:Calorimetry; D003062:Codon / Q000235:genetics*; D006160:Guanosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics*; D012343:RNA, Transfer / Q000235:genetics*; D012346:RNA, Transfer, Amino Acyl / Q000235:genetics* / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*
D000926:Anticodon; D001426:Bacterial Proteins; D003062:Codon; D010445:Peptide Elongation Factors; D012333:RNA, Messenger; D012346:RNA, Transfer, Amino Acyl; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D010444:Peptide Elongation Factor Tu; D008274:Magnesium
Mekhanizm kodon-antikodonnogo vsaimodeĭstviia v ribosomakh. Vzaimodeĭstvie aminoatsil-tRNA s 70S ribosomami Escherichia coli v otsutstvie faktora élongatsii EF-Tu i GTP.