Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 108; no. 13; pp. 5215 - 5220
• Main Authors: Schrader, Jared M, Chapman, Stephen J, Uhlenbeck, Olke C
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 29.03.2011; National Acad Sciences
• Subjects: Amino acids; Bacteria; Bacterial proteins; Base Sequence; Binding sites; Biochemistry; Biological Sciences; Chimeras; codons; crystal structure; E coli; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; esterification; Hydrogen bonds; Hydrolysis; Models, Molecular; Molecular Sequence Data; mutants; Mutation; Nucleic Acid Conformation; Peptide Elongation Factor Tu - genetics; Peptide Elongation Factor Tu - metabolism; Peptide elongation factors; Peptides; Protein Binding; Protein Biosynthesis; Protein Conformation; Ribosomes; Ribosomes - metabolism; RNA, Transfer, Amino Acyl - genetics; RNA, Transfer, Amino Acyl - metabolism; Standard error; Thermodynamics; Transfer RNA

To better understand why aminoacyl-tRNAs (aa-tRNAs) have evolved to bind bacterial elongation factor Tu (EF-Tu) with uniform affinities, mutant tRNAs with differing affinities for EF-Tu were assayed for decoding on Escherichia coli ribosomes. At saturating EF-Tu concentrations, weaker-binding aa-tRN...