title: Predicting the binding affinities of misacylated tRNAs for Thermus thermophilus EF-Tu.GTP.
abstract: The free energies for the binding of 20 different unmodified Escherichia coli elongator aminoacyl-tRNAs to Thermus thermophilus elongation factor Tu (EF-Tu) were determined. When combined with the binding free energies for the same tRNA bodies misacylated with either valine or phenylalanine determined previously [Asahara, H., and Uhlenbeck, O. C. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 3499-3504], these data permit the calculation of the contribution of each esterified amino acid to the total free energy of binding of the complex. The two data sets can also be used to calculate the free energy of binding of EF-Tu to any misacylated E. coli tRNA, and the values agree well with previously published experimental values. In addition, a survey of active misacylated suppressor tRNAs suggests that a minimal threshold of binding free energy for EF-Tu is required for suppression to occur.
authors.affiliation: Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, 2205 Tech Drive, Hogan 2-100, Evanston, Illinois 60208, USA.
authors.forename: Haruichi
authors.initials: H
authors.lastname: Asahara
authors.forename: Olke C
authors.initials: OC
authors.lastname: Uhlenbeck
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry*; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D011237:Predictive Value of Tests; D011485:Protein Binding / Q000502:physiology; D012329:RNA, Bacterial / Q000737:chemistry*; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics; D016963:Thermus thermophilus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012346:RNA, Transfer, Amino Acyl; D010444:Peptide Elongation Factor Tu