The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (Q73385508)

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3 November 2019

title

The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (English)

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3 November 2019

author name string

E L Vorstenbosch

1

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3 November 2019

A P Potapov

2

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3 November 2019

J M de Graaf

3

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3 November 2019

B Kraal

4

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3 November 2019

publication date

1 January 2000

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3 November 2019

published in

Journal of Proteomics

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3 November 2019

volume

42

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3 November 2019

issue

1-2

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3 November 2019

page(s)

1-14

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Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli

3 November 2019

cites work

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Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog

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7 January 2021

The determination of binding parameters from protection experiments. A quantitative assay for ternary complex formation of elongation factor Tu, GTP, and aminoacyl-tRNA.

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Aminoacyl transfer ribonucleic acid binding site of the bacterial elongation factor Tu

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The complex formation between Escherichia coli aminoacyl-tRNA, elongation factor Tu and GTP. The effect of the side-chain of the amino acid linked to tRNA

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7 January 2021

Mutants of EF-Tu defective in binding aminoacyl-tRNA.

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Discrimination between aminoacyl groups on su+ 7 tRNA by elongation factor Tu

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7 January 2021

Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes

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7 January 2021

Interaction of aminoacyl-tRNA with bacterial elongation factor Tu: GTP complex: effects of the amino group of amino acid esterified to tRNA, the amino acid side chain, and tRNA structure

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7 January 2021

Direct determination of the association constant between elongation factor Tu X GTP and aminoacyl-tRNA using fluorescence.

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7 January 2021

Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis.

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Interaction of elongation factor Tu from Escherichia coli with aminoacyl-tRNA carrying a fluorescent reporter group on the 3' terminus.

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7 January 2021

Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu.

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7 January 2021

A second tRNA binding site on elongation factor Tu is induced while the factor is bound to the ribosome

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7 January 2021

Pulvomycin-resistant mutants of E.coli elongation factor Tu.

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7 January 2021

Substitution of Arg230 and Arg233 in Escherichia coli elongation factor Tu strongly enhances its pulvomycin resistance

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7 January 2021

Isolation and functional analysis of histidine-tagged elongation factor Tu

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7 January 2021

Divergent effects of fluoroaluminates on the peptide chain elongation factors EF-Tu and EF-G as members of the GTPase superfamily.

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7 January 2021

An Algorithm for Least-Squares Estimation of Nonlinear Parameters

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7 January 2021

Ternary Complex Formation between Elongation Factor Tu, GTP and Aminoacyl-tRNA: an Equilibrium Study

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7 January 2021

Crystal structure of active elongation factor Tu reveals major domain rearrangements

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7 January 2021

Escherichia coli elongation-factor-Tu mutants with decreased affinity for aminoacyl-tRNA.

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7 January 2021

A growth-defective kirromycin-resistant EF-Tu Escherichia coli mutant and a spontaneously evolved suppression of the defect.

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7 January 2021

Translational activities of EF-Tu [G222D] which cannot be reconciled with the classical scheme of the polypeptide chain elongation cycle.

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7 January 2021

10.1016/S0165-022X(99)00032-9

Identifiers

DOI

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3 November 2019

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