Mutants of EF-Tu defective in binding aminoacyl-tRNA

FEBS Letters
F AbdulkarimD Hughes

Abstract

Five single amino acid substitution variants of EF-Tu from Salmonella typhimurium were tested for their ability to promote poly(U)-translation in vitro. The substitutions are Leu120 Gln, Gln124 Arg and Tyr160 (Asp or Asn or Cys). They were selected by their kirromycin resistant phenotypes and all substitutions are in domain I at the interface between domains I and III of the EF-Tu.GTP configuration. The different EF-Tu variants exhibit a spectrum of phenotypes. First, k cat/K(M) for the interaction between ternary complex and the programmed ribosome is apparently reduced by the substitutions Leu120 Gln, Gln124 Arg and Tyr160 Cys. Second, this reduction is caused by a defect in the interaction between these EF-Tu variants and aminoacyl-tRNA during translation. Third, in four cases out of five the affinity of the complex between EF-Tu.GTP and aminoacyl-tRNA is significantly decreased. The most drastic reduction is observed for the Gln124 Arg change, where the association constant is 30-fold lower than in the wild-type case. Fourth, missense errors are increased as well as decreased by the different amino acid substitutions. Finally, the dissociation rate constant (kd) for the release of GDP from EF-Tu is increased 6-fold by the T...Continue Reading

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Citations

Dec 5, 1998·Biochimica Et Biophysica Acta·I M Krab, A Parmeggiani
Feb 1, 1997·Current Opinion in Structural Biology·B F Clark, J Nyborg
Mar 4, 2014·PloS One·Jessica M BergmanDiarmaid Hughes
Jul 25, 1998·FEBS Letters·J Nyborg, A Liljas

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