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The elongation factor tu from escherichia coli aminoacyl transfer rna and guanosine tetra phosphate form a ternary complex which is bound by programmed ribosomes



The elongation factor tu from escherichia coli aminoacyl transfer rna and guanosine tetra phosphate form a ternary complex which is bound by programmed ribosomes



Journal of Biological Chemistry 258(23): 14200-14205



The interaction of the E. coli elongation factor Tu guanosine tetraphosphate complex (EF-Tu.cntdot.ppGpp) with aminoacyl-tRNA (aa-tRNA) was reinvestigated by gel filtration and hydrolysis protection experiments. EF-Tu.cntdot.ppGpp like EF-Tu.cntdot.GDP forms a fairly stable complex with Phe-tRNAPhe, KAss being 0.6 .times. 105 M-1 at 25.degree. C. The binding of the EF-Tu.cntdot.ppGpp.cntdot.aa-tRNA complex to programmed ribosomes was investigated by a centrifugation technique. This complex is bound codon-specific with KAss = 3 .times. 107 M at 0.degree. C and stimulates peptidyl transfer. A numerical estimation of the intracellular concentration of EF-Tu.cntdot.GTP.cntdot.aa-tRNA and EF-Tu.cntdot.aa-tRNA during normal growth and under the stringent response indicates that ppGpp accumulation does affect the EF-Tu.cntdot.GP.cntdot.aa-tRNA concentration but does not lead to major depletion of this pool. Due to the higher affinity of EF-Tu.cntdot.GTP to aa-tRNA and of the ternary complex EF-Tu.cntdot.GTP.cntdot.aa-tRNA to the ribosome, EF-Tu.cntdot.ppGpp.cntdot.aa-tRNA binding to the ribosome is not significant. According to the measurements and calculations, a direct participation of EF-Tu in slowing down the rate of protein biosynthesis and improving its accuracy during amino acid starvation is not obvious.

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