1998
DOI: 10.1016/s0167-4781(98)00169-9
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EF-Tu, a GTPase odyssey

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Cited by 106 publications
(93 citation statements)
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“…The fraction of [ 3 H]-aa-tRNA bound by EF-Tu over time was fit to a single exponential using Kaleidagraph. tRNA mutations with k off values greater than 0.02 s −1 or less than 0.0002 s −1 were measured at multiple lower or higher NH 4 Cl concentrations, and their k off was extrapolated to 70 mM NH 4 Cl present in RB (12). All measurements were performed in triplicate.…”
Section: Methodsmentioning
confidence: 99%
See 1 more Smart Citation
“…The fraction of [ 3 H]-aa-tRNA bound by EF-Tu over time was fit to a single exponential using Kaleidagraph. tRNA mutations with k off values greater than 0.02 s −1 or less than 0.0002 s −1 were measured at multiple lower or higher NH 4 Cl concentrations, and their k off was extrapolated to 70 mM NH 4 Cl present in RB (12). All measurements were performed in triplicate.…”
Section: Methodsmentioning
confidence: 99%
“…T he ternary complex of bacterial elongation factor Tu (EF-Tu), GTP and aminoacyl-tRNA (aa-tRNA) binds to the ribosome and participates in a multistep decoding pathway in which GTP is hydrolyzed, EF-Tu•GDP is released, and the aa-tRNA enters the ribosomal A site (1)(2)(3)(4)(5)(6). Although all elongator aa-tRNAs bind EF-Tu•GTP with similar affinities (7)(8)(9), studies with misacylated tRNAs reveal that the protein shows substantial specificity for both the esterified amino acid and the tRNA body (10)(11)(12).…”
mentioning
confidence: 99%
“…Assuming a concentration of a few µM for typical ternary complex species [53], binding to the ribosome is expected to occur with rate ∼ 10 s −1 [29]. Thus, peptide chain elongation may proceed rather close to the diffusion limit and the large concentration of ternary complexes in cells (EF-Tu is the most abundant protein in E. coli cells [30]) is likely required to avoid such limitation to ensure efficient cellular use of ribosomes. Indeed, from a proteome partitioning point of view, the optimal solution would be to set the Michaelis constant of translation elongation as low as possible.…”
Section: Translationmentioning
confidence: 99%
“…As a consequence, reactions are expected to be diffusion-limited or close to the diffusion limit. Specifically for ribosomes, it was recently proposed that the slow diffusion of ternary complexes (tRNAs charged with amino acids and GTP-activated elongation factor Tu) imposes a fundamental limitation on the speed of translation, which necessitates the large concentrations of elongation factors in rapidly growing bacteria [29] (elongation factor Tu is the most abundant protein in E. coli [30]). Such a limitation would be aggravated during growth under increased osmotic pressure.…”
Section: Introductionmentioning
confidence: 99%
“…As a member of the GTPase-switch protein family, EF-Tu is cycling between different conformations and interacts with partners such as GDP or GTP, aa-tRNA, elongation factor Ts (EF-Ts) and ribosomes (reviewed in [1]). High-resolution crystallographic structures of many of these complexes have been elucidated [2±7].…”
mentioning
confidence: 99%