[Ef-Ts elongation factor interacts with elongation factor EF-Tu on ribosomes prior to the GTP hydrolysis stage].
Methods of high-speed centrifugation and limited proteolysis were used to probe the interaction of EF-Tu with EF-Ts on the ribosome. It is shown that EF-Ts dissociates from EF-Tu only after EF-Tu-mediated GTP hydrolysis, i.e. EF-Ts within the EF-Tu.ribosome complexes in the pre-GTP-hydrolysis state co-sediments with the ribosomes and its rate of proteolysis is distinct from that of free EF-Ts. Moreover, as seen from the difference in sensitivity to trypsin of ribosomal proteins L19 and L27 EF-Ts affects the interaction of EF-Tu with the ribosome.
Bubunenko
M G
MG
Gudkov
A T
AT
D004591:Electrophoresis, Polyacrylamide Gel; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006868:Hydrolysis; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D010445:Peptide Elongation Factors / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D014357:Trypsin
D010445:Peptide Elongation Factors; C023512:elongation factor Ts; D006160:Guanosine Triphosphate; D014357:Trypsin; D010444:Peptide Elongation Factor Tu
Faktor élongatsii EF-Ts vzaimodeĭstvuet s faktorom élongatsii EF-Tu na ribosomakh do stadii gidroliza GTP.