Time-resolved fluorescence studies on the ternary complex formed between bacterial elongation factor Tu, guanosine 5'-triphosphate, and phenylalanyl-tRNAPhe

Biochemistry ◽  
1989 ◽  
Vol 28 (9) ◽  
pp. 4109-4117 ◽  
Author(s):  
Theodore L. Hazlett ◽  
Arthur E. Johnson ◽  
David M. Jameson
Keyword(s):  
Ternary Complex ◽  
Elongation Factor ◽  
Elongation Factor Tu ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Studies

Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: mechanism and GTP consumption

1995 ◽  
Vol 73 (11-12) ◽  
pp. 1221-1227 ◽  
Author(s):  
Marina V. Rodnina ◽  
Tillmann Pape ◽  
Rainer Fricke ◽  
Wolfgang Wintermeyer
Keyword(s):  
Ternary Complex ◽  
Elongation Factor ◽  
Peptide Bond ◽  
Elongation Factor Tu ◽  
Gtp Hydrolysis ◽  
Time Resolved ◽  
Codon Recognition ◽  
Fluorescence Measurements ◽  
A Site

The mechanism of elongation factor Tu (EF-Tu) catalyzed aminoacyl-tRNA (aa-tRNA) binding to the A site of the ribosome was studied. Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu∙GTP∙aa-tRNA (ternary) and (EF-Tu∙GTP)2∙aa-tRNA (quinternary), can be formed in vitro depending on the conditions. On interaction with the ribosomal A site, generally only one molecule of GTP is hydrolysed per aa-tRNA bound and peptide bond formed. The second GTP molecule from the quinternary complex is hydrolyzed only during translation of an oligo(U) tract in the presence of EF-G. The first step in the interaction between the ribosome and the ternary complex is the codon-independent formation of an initial complex. In the absence of codon recognition, the aa-tRNA–EF-Tu complex does not enter further steps of A site binding and remains in the initial binding state. Despite the rapid formation of the initial complex, the rate constant of GTP hydrolysis in the noncognate complex is four orders of magnitude lower compared with the cognate complex. This, together with the results of time-resolved fluorescence measurements, suggests that codon recognition by the ternary complex on the ribosome initiates a series of structural rearrangements that result in a conformational change of EF-Tu, presumably involving the effector region, which, in turn, triggers GTP hydrolysis and the subsequent steps of A site binding.Key words: translation, A site, codon recognition, fluorescence, stopped-flow.

Time-resolved Fluorescence Studies of the Molten Globule State of Apomyoglobin

1996 ◽  
Vol 257 (4) ◽  
pp. 877-885 ◽  
Author(s):  
Christian Rischel ◽  
Per Thyberg ◽  
Rudolf Rigler ◽  
Flemming M. Poulsen
Keyword(s):  
Molten Globule ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Molten Globule State ◽  
Fluorescence Studies

Time-Resolved Fluorescence Studies on Exciplexes

1972 ◽  
Vol 79 (3_4) ◽  
pp. 150-167 ◽  
Author(s):  
Nobuaki Nakashima ◽  
Noboru Mataga ◽  
Fusao Ushio ◽  
Chiyoe Yamanaka
Keyword(s):  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Studies

Time-resolved fluorescence studies on the single tryptophan in bovine brain S-100a protein

1990 ◽  
Author(s):  
Chien-Kao Wang ◽  
Rajam S. Mani ◽  
Cyril M. Kay ◽  
Herbert C. Cheung
Keyword(s):  
Bovine Brain ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Studies

Steady-state and time-resolved fluorescence studies on interactions of carbon “quantum” dots with nitrotoluenes

2017 ◽  
Vol 468 ◽  
pp. 300-307 ◽  
Author(s):  
Gregory E. LeCroy ◽  
K.A. Shiral Fernando ◽  
Christopher E. Bunker ◽  
Ping Wang ◽  
Nicholas Tomlinson ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Steady State ◽  
Carbon Quantum Dots ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Studies
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