The elongation factor Tu from Escherichia coli, aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is bound by programmed ribosomes.-Reference-Cited by-同舟云学术

The elongation factor Tu from Escherichia coli, aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is bound by programmed ribosomes.

Published:1983-12 Issue:23 Volume:258 Page:14200-14205
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Pingoud A,Gast F U,Block W,Peters F

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. REGULATION OF BACTERIAL ppGpp AND pppGpp

2. STRINGENT CONTROL IN E. COLI

3. The interaction of guanosine 5′-diphosphate, 2′ (3′)-diphosphate with the bacterial elongation factor Tu

4. The Elongation Factor Tu . Guanosine Tetraphosphate Complex

5. X-ray determination of the GDP-binding site of Escherichia coli elongation factor Tu by substitution with ppGpp

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1. The Ribosome as a Switchboard for Bacterial Stress Response;Frontiers in Microbiology;2021-01-08

2. Elongation Factor Tu’s Nucleotide Binding Is Governed by a Thermodynamic Landscape Unique among Bacterial Translation Factors;Journal of the American Chemical Society;2019-05-06

3. Kinetics of d-Amino Acid Incorporation in Translation;ACS Chemical Biology;2019-01-16

4. The C-terminal Helix of Pseudomonas aeruginosa Elongation Factor Ts Tunes EF-Tu Dynamics to Modulate Nucleotide Exchange;Journal of Biological Chemistry;2016-10

5. Direct binding targets of the stringent response alarmone (p)ppGpp;Molecular Microbiology;2012-08-02