Effects of nucleotide- and aurodox-induced changes in elongation factor Tu conformation upon its interactions with aminoacyl transfer RNA. A fluorescence study

Biochemistry ◽  
1990 ◽  
Vol 29 (7) ◽  
pp. 1757-1763 ◽  
Author(s):  
V. Ann Dell ◽  
David L. Miller ◽  
Arthur E. Johnson
Keyword(s):  
Elongation Factor ◽  
Transfer Rna ◽  
Elongation Factor Tu ◽  
Fluorescence Study ◽  
Aminoacyl Transfer ◽  
Induced Changes

scholarly journals The Role of Guanosine Triphosphate Hydrolysis in Elongation Factor Tu-promoted Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes

1973 ◽  
Vol 248 (1) ◽  
pp. 375-377 ◽  
Author(s):  
Hideyoshi Yokosawa ◽  
Noriko Inoue-Yokosawa ◽  
Ken-Ichi Arai ◽  
Masao Kawakita ◽  
Yoshito Kaziro
Keyword(s):  
Ribonucleic Acid ◽  
Elongation Factor ◽  
Elongation Factor Tu ◽  
Guanosine Triphosphate ◽  
Aminoacyl Transfer

scholarly journals A recent intermezzo at the Ribosome Club

2017 ◽  
Vol 372 (1716) ◽  
pp. 20160185 ◽  
Author(s):  
Michael Y. Pavlov ◽  
Anders Liljas ◽  
Måns Ehrenberg
Keyword(s):  
Messenger Rna ◽  
Ternary Complex ◽  
Elongation Factor ◽  
Transfer Rna ◽  
Elongation Factor Tu ◽  
Transfer Rnas ◽  
30S Subunit ◽  
Translation Accuracy ◽  
Codon Selection ◽  
Two Sides

Two sets of ribosome structures have recently led to two different interpretations of what limits the accuracy of codon translation by transfer RNAs. In this review, inspired by this intermezzo at the Ribosome Club, we briefly discuss accuracy amplification by energy driven proofreading and its implementation in genetic code translation. We further discuss general ways by which the monitoring bases of 16S rRNA may enhance the ultimate accuracy ( d -values) and how the codon translation accuracy is reduced by the actions of Mg 2+ ions and the presence of error inducing aminoglycoside antibiotics. We demonstrate that complete freezing-in of cognate-like tautomeric states of ribosome-bound nucleotide bases in transfer RNA or messenger RNA is not compatible with recent experiments on initial codon selection by transfer RNA in ternary complex with elongation factor Tu and GTP. From these considerations, we suggest that the sets of 30S subunit structures from the Ramakrishnan group and 70S structures from the Yusupov/Yusupova group may, after all, reflect two sides of the same coin and how the structurally based intermezzo at the Ribosome Club may be resolved simply by taking the dynamic aspects of ribosome function into account. This article is part of the themed issue ‘Perspectives on the ribosome’.

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

Biochemistry ◽  
1981 ◽  
Vol 20 (16) ◽  
pp. 4663-4666 ◽  
Author(s):  
Lawrence K. Duffy ◽  
Louise Gerber ◽  
Arthur E. Johnson ◽  
David L. Miller
Keyword(s):  
Binding Site ◽  
Ribonucleic Acid ◽  
Elongation Factor ◽  
Elongation Factor Tu ◽  
Histidine Residue ◽  
Aminoacyl Transfer

scholarly journals Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

2009 ◽  
Vol 106 (4) ◽  
pp. 1063-1068 ◽  
Author(s):  
E. Villa ◽  
J. Sengupta ◽  
L. G. Trabuco ◽  
J. LeBarron ◽  
W. T. Baxter ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Elongation Factor Tu ◽  
Gtp Hydrolysis ◽  
Induced Changes
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