[Mechanism of codon-anticodon interaction in ribosomes. Interaction of aminoacyl-tRNA with 70S ribosomes in the absence of elongation factor EF-Tu and GTP]

Mol Biol (Mosk). 1981 Jul-Aug;15(4):779-89.
[Article in Russian]

Abstract

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.

Publication types

  • English Abstract

MeSH terms

  • Anticodon / genetics*
  • Bacterial Proteins / metabolism
  • Calorimetry
  • Codon / genetics*
  • Guanosine Triphosphate / metabolism
  • Kinetics
  • Magnesium / pharmacology
  • Peptide Elongation Factor Tu
  • Peptide Elongation Factors / metabolism
  • RNA, Messenger / genetics*
  • RNA, Transfer / genetics*
  • RNA, Transfer, Amino Acyl / genetics*
  • RNA, Transfer, Amino Acyl / metabolism
  • Ribosomes / metabolism*

Substances

  • Anticodon
  • Bacterial Proteins
  • Codon
  • Peptide Elongation Factors
  • RNA, Messenger
  • RNA, Transfer, Amino Acyl
  • Guanosine Triphosphate
  • RNA, Transfer
  • Peptide Elongation Factor Tu
  • Magnesium