Year: 2014
Type: article
Abstract: During protein synthesis, elongation factor-Tu (EF-Tu) bound to GTP chaperones the entry of aminoacyl-tRNA (aa-tRNA) into actively translating ribosomes. In so doing, EF-Tu increases the rate and fidelity of the translation mechanism. Recent evidence suggests that EF-Ts, the guanosine nucleotide exchange factor for EF-Tu, directly accelerates both the formation and dissociation of the EF-Tu-GTP-Phe-tRNA(Phe) ternary complex (Burnett, B. J., Altman, R. B., Ferrao, R., Alejo, J. L., Kaur, N., Kanji, J., and Blanchard, S. C. (2013) J. Biol. Chem. 288, 13917-13928). A central feature of this model is the existence of a quaternary complex of EF-Tu/Ts·GTP·aa-tRNA(aa). Here, through comparative investigations of phenylalanyl, methionyl, and arginyl ternary complexes, and the development of a strategy to monitor their formation and decay using fluorescence resonance energy transfer, we reveal the generality of this newly described EF-Ts function and the first direct evidence of the transient quaternary complex species. These findings suggest that EF-Ts may regulate ternary complex abundance in the cell through mechanisms that are distinct from its guanosine nucleotide exchange factor functions.
Source: Journal of Biological Chemistry
Authors: Benjamin J. Burnett, Roger B. Altman, Angelica Ferguson, Michael R. Wasserman, Zhou Zhou, Scott C. Blanchard
Institution: Weill Cornell Medicine
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Awards: G1390803635, smFRET Investigation of Aminoglycoside-induced Ototoxicity, G2791615253, Imaging Protein Synthesis on the Ribosome using Single-Molecule FRET, Quantitative investigations of transporter dynamics and uptake at the single-mole, G4769796230, Next-generation fluorescent Probes for Biological research
OpenAlex ID: W2360859268