title: Direct evidence of an elongation factor-Tu/Ts·GTP·Aminoacyl-tRNA quaternary complex.
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.
authors.affiliation: From the Department of Physiology and Biophysics and.
authors.forename: Benjamin J
authors.initials: BJ
authors.lastname: Burnett
authors.affiliation: From the Department of Physiology and Biophysics and.
authors.forename: Roger B
authors.initials: RB
authors.lastname: Altman
authors.affiliation: Tri-Institutional Program in Chemical Biology, Weill Cornell Medical College, New York, New York 10065.
authors.forename: Angelica
authors.initials: A
authors.lastname: Ferguson
authors.affiliation: From the Department of Physiology and Biophysics and.
authors.forename: Michael R
authors.initials: MR
authors.lastname: Wasserman
authors.affiliation: From the Department of Physiology and Biophysics and.
authors.forename: Zhou
authors.initials: Z
authors.lastname: Zhou
authors.affiliation: From the Department of Physiology and Biophysics and Tri-Institutional Program in Chemical Biology, Weill Cornell Medical College, New York, New York 10065 scb2005@med.cornell.edu.
authors.forename: Scott C
authors.initials: SC
authors.lastname: Blanchard
mesh_terms: D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D008958:Models, Molecular; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism*; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; C023512:elongation factor Ts; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu
keywords: Elongation Factor Ts; Elongation Factor Tu; G Protein; Guanine Nucleotide Exchange Factor (GEF); Guanosine Nucleotide Exchange Factor; Protein Synthesis; Ternary Complex; Translation; Translation Elongation Factor