PMID:9325093

Citation	Saarma, U, Remme, J, Ehrenberg, M and Bilgin, N (1997) An A to U transversion at position 1067 of 23 S rRNA from Escherichia coli impairs EF-Tu and EF-G function. J. Mol. Biol. 272:327-35
Abstract	Escherichia coli ribosomes with an A to U transversion at nucleotide 1067 of their 23 S rRNA are impaired in their effective association rate constants (kcat/KM) for both EF-Tu and EF-G binding. In addition, the times that EF-G and EF-Tu spend on the ribosome during elongation are significantly increased by the A to U transversion. The U1067 mutation impairs EF-Tu function more than EF-G function. The increase in the time that EF-Tu remains bound to ribosome is caused, both by a slower rate of GTP-hydrolysis in ternary complex and by a slower EF-Tu.GDP release from the mutated ribosomes. There is, at the same time, no change in ribosomal accuracy for aminoacyl-tRNA recognition. With support from these new data we propose that nucleotide 1067 is part of the ribosomal A-site where it directly interacts with both EF-G and EF-Tu.
Links	PubMed Online version:10.1006/jmbi.1997.1254
Keywords	Adenine; Escherichia coli/genetics; Guanosine Triphosphate/metabolism; Hydrolysis; Kinetics; Mutation; Peptide Chain Elongation, Translational/genetics; Peptide Elongation Factor G; Peptide Elongation Factor Tu/metabolism; Peptide Elongation Factors/metabolism; RNA, Ribosomal, 23S/genetics; RNA, Ribosomal, 23S/metabolism; RNA, Transfer, Amino Acyl/metabolism; Ribosomes/genetics; Ribosomes/metabolism; Uridine
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