GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site (Q35613520)

9 August 2017

title

GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site (English)

1 reference

9 August 2017

J M Van Noort

1

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9 August 2017

B Kraal

series ordinal

2

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9 August 2017

L Bosch

series ordinal

3

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9 August 2017

language of work or name

English

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publication date

1 July 1986

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9 August 2017

number of pages

5

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Proceedings of the National Academy of Sciences of the United States of America

inferred from page(s)

published in

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9 August 2017

volume

83

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9 August 2017

issue

13

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9 August 2017

page(s)

4617-4621

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Hydrolysis of GTP on elongation factor Tu.ribosome complexes promoted by 2'(3')-O-L-phenylalanyladenosine

9 August 2017

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Stimulation of Escherichia coli elongation factor Tu-dependent GTP hydrolysis by aminoacyl oligonucleotides in the presence of aurodox

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

The elongation factor Tu.kirromycin complex has two binding sites for tRNA molecules.

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Structural variability of tRNA: small-angle x-ray scattering of the yeast tRNAphe-Escherichia coli tRNAGlu2 complex

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

The accuracy of protein biosynthesis is limited by its speed: high fidelity selection by ribosomes of aminoacyl-tRNA ternary complexes containing GTP[gamma S].

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Structure-function relations in E. coli 16S RNA.

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Cross-linking of tRNA at two different sites of the elongation factor Tu.

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Properties and regulation of the GTPase activities of elongation factors Tu and G, and of initiation factor 2

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Complementary Oligonucleotide Binding to the Anticodon Loop of fMet-transfer RNA

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

The Stability of a Codon Transfer RNA Complex

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

44 Assay for nonenzymatic and enzymatic translocation with Escherichia coli ribosomes

12 July 2018

1 reference

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Interaction of siomycin with the acceptor site of Escherichia coli ribosomes.

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Ribosomes cannot interact simultaneously with elongation factors EF Tu and EF G.

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Kinetic Proofreading: A New Mechanism for Reducing Errors in Biosynthetic Processes Requiring High Specificity

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Kirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Mutants of the elongation factor EF-Tu, a new class of nonsense suppressors

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

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

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Interaction of unfolded tRNA with the 3'-terminal region of E. coli 16S ribosomal RNA.

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

The Binding of Kirromycin to Elongation Factor Tu. Structural Alterations are Responsible for the Inhibitory Action

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

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

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Modification of Elongation-Factor-Tu . Guanine-Nucleotide Interaction by Kirromycin. A Comparison with the Effect of Aminoacyl-tRNA and Elongation Factor Ts

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Effect of Kirromycin on Elongation Factor Tu. Location of the Catalytic Center for Ribosome . Elongation-Factor-Tu GTPase Activity on the Elongation Factor

12 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

Mode of action of N-tosyl-L-phenylalanylchloromethane on the elongation protein-synthesizing S 3 factor from Bacillus stearothermophilus

12 July 2018

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=323792

25 September 2018

12 December 2020

A semi-quantitative treatment of missense and nonsense suppression in the strA and ram ribosomal mutants of Escherichia coli Evaluation of some molecular parameters of translation in vivo

1 reference

12 December 2020

Studies on the polypeptide elongation factors form E. coli. VI. Characterization of sulfhydryl groups in EF-Tu and EF-Ts

1 reference

12 December 2020

A simplified procedure for the isolation of bacterial polypeptide elongation factor EF-Tu

1 reference

12 December 2020

Multistep mechanism of codon recognition by transfer ribonucleic acid

1 reference

12 December 2020

Energetic aspects of the EF-Tu-dependent GTPase activity. A study using the antibiotic kirromycin

1 reference

12 December 2020

The GTPase activity of elongation factor Tu and the 3'-terminal end of aminoacyl-tRNA

1 reference

12 December 2020

Effects of Antibiotics, N-Acetylaminoacyl-tRNA and Other Agents on the Elongation-Factor-Tu Dependent and Ribosome-Dependent GTP Hydrolysis Promoted by 2′(3′)-O-l-Phenylalanyladenosine

1 reference

12 December 2020

Modulation by monovalent and divalent cations of the guanosine-5'-triphosphatase activity dependent on elongation factor Tu

1 reference

12 December 2020

Elongation factor Tu.ribosome dependent guanosine 5'-triphosphate hydrolysis: elucidation of the role of the aminoacyl transfer ribonucleic acid 3' terminus and site(s) involved in the inducing of the guanosinetriphosphatase reaction

1 reference

12 December 2020

Effect of thiostrepton and 3'-terminal fragments of aminoacyl-tRNA on EF-Tu and ribosome-dependent GTP hydrolysis

1 reference

12 December 2020

Different regions of aminoacyl-tRNA regulate the function of elongation factor Tu

1 reference

12 December 2020

N-Tosyl-L-phenylalanylchloromethane reacts with cysteine 81 in the molecule of elongation factor Tu from Escherichia coli

1 reference

12 December 2020

Interaction between the Different Domains of Aminoacyl-tRNA and the Elongation-Factor-Tu . Kirromycin Complex

1 reference

12 December 2020

Codon-induced transfer RNA association. A property of transfer RNA involved in its adaptor function?

1 reference

12 December 2020

Transfer ribonucleic acid deprived of the C-C-A 3'-extremity can interact with elongation factor Tu

1 reference

12 December 2020

Mechanism of codon recognition by transfer RNA and codon-induced tRNA association

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.83.13.4617

1 reference

9 August 2017

1 reference

9 August 2017

1 reference