[Stoichiometry of GTP hydrolysis during peptide synthesis on the ribosome. GTP hydrolysis uncoupled with ribosomal peptide synthesis and dependent on preparation of elongation factor T].
It is shown that preparations of EF-T are practically free from GTPase activity, if they were formed from EF-Tu and EF-Ts carefully purified from GTPase beforehand. Some Ef-T-dependent GTPase can arise after addition of tRNA or aminoacyl-tRNA preparations to a EF-T+ribosomes mixture. Poly(U) stimulates, as a rule, EF-T-dependent GTPase in the EF-T/ribosomes+tRNA mixture. Uncoupled EF-T-dependent GTPase of the EF-T+ribosomes+tRNA+poly(U) mixture is by 1--2 orders of magnitude less than uncoupled EF-G-dependent GTPase under the same conditions. A conclusion is made that uncoupled EF-T-dependent GTPase is an inevitable obstacle when studying the GTP expenditure in the process of ribosomal protein synthesis, if a traditional cell-free protein-synthesizing system is used for this purpose.
D004926:Escherichia coli / Q000235:genetics*; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism*; D010441:Peptide Chain Elongation, Translational; D010445:Peptide Elongation Factors / Q000378:metabolism*; D010455:Peptides / Q000235:genetics*; D014176:Protein Biosynthesis; D012343:RNA, Transfer / Q000235:genetics; D012346:RNA, Transfer, Amino Acyl / Q000235:genetics; D012270:Ribosomes / Q000378:metabolism*
D010445:Peptide Elongation Factors; D010455:Peptides; D012346:RNA, Transfer, Amino Acyl; C036506:elongation factor T; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D020963:GTP Phosphohydrolase-Linked Elongation Factors
Izuchenie stekhiometrii raspada GTP pri sinteze peptida na ribosome. Gidroliz GTP, ne sopriazhennyĭ s sintezom peptida i zavisimĭ ot preparata faktora elongatsii T.