title: [Effect of the concentration ratio of bi- and monovalent ions on the functional activity of 30S ribosome subunits of Escherichia coli].
abstract: Experiments on poly(U)-dependent binding of Phe-tRNAPhe to 30S subunits revealed the existence of a critical [Mg2+]/[NH4+] ratio in a medium (approximately 0.05-0.1) with respect to the binding capacity of subunits. If the ratio is greater than the critical one, 30S subunits undergo reversible inactivation even at the highest Mg2+ concentrations (up to 20 mM). The stronger is the deviation from the [Mg2+]/[NH4+] value = 0.05-0.1, the greater are both the rate and extent of such an inactivation. Two sites for tRNA in initially active 30S subunits have been shown to be inactivated in an interdependent way. On the other hand, a progressive decrease of [Mg2+]/[NH4+] ratio in a medium (from the value of 0.05 and lower) does not produce inactivation, but rather results in reduced affinity constants of Phe-tRNAPhe for active sites of 30S subunits.
mesh_terms: D002413:Cations, Divalent / Q000494:pharmacology*; D002414:Cations, Monovalent / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D006358:Hot Temperature; D007700:Kinetics; D012346:RNA, Transfer, Amino Acyl / Q000096:biosynthesis; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*
chemical_list: D002413:Cations, Divalent; D002414:Cations, Monovalent; D012346:RNA, Transfer, Amino Acyl; D012269:Ribosomal Proteins; C040469:ribosomal protein S30
vernacular_title: Vliianie sootnosheniia kontsentratsii dvukh- i odnovalentnykh kationov na funktsional'nuiu aktivnost' 30S subchastits ribosom Escherichia coli.