Identification of thermodynamically relevant interactions between EF-Tu and backbone elements of tRNA

Journal of Molecular Biology

Volumn 308, Issue 5, 2001, Pages 895-905

  Pleiss, Jeffrey A ^a   Uhlenbeck, Olke C ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

Conformational rearrangements; Deoxynucleotide substitutions; Elongation factor Tu (EF Tu); Thermodynamic footprinting; tRNA

Indexed keywords

DEOXYRIBONUCLEOTIDE; ELONGATION FACTOR TU; TRANSFER RNA;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN RNA BINDING; PROTEIN STRUCTURE; RNA SEQUENCE; RNA STRUCTURE; STRUCTURE ANALYSIS; THERMODYNAMICS; THERMUS AQUATICUS; THERMUS THERMOPHILUS;

THERMUS AQUATICUS; THERMUS THERMOPHILUS;

EID: 0035906732     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4612     Document Type: Article

References (45)

1. Changes in aminoacyl transfer ribonucleic acid conformation upon association with elongation factor Tu-guanosine 5′-triphosphate. Fluorescence studies of ternary complex conformation and topology
2. Overproduction of the Thermus thermophilus elongation factor Tu in Escherichia coli
3. Both positional isomers of aminoacyl-tRNA's are bound by elongation factor Tu
4. The role of 2′-hydroxyl groups in an RNA-protein interaction
5. Aminoacyl-tRNAs. Diversity before and unity after interaction with EF-Tu:GTP
6. Phe mutants
7. Minor-groove recognition of double-stranded RNA by the double- stranded RNA-binding domain from the RNA-activated protein kinase PKR
8. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
9. Quantitative assessment of EF-1alpha. GTP binding to aminoacyl-tRNAs, aminoacyl-viral RNA, and tRNA shows close correspondence to the RNA binding properties of EF-Tu
10. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
11. Effector region of the translation elongation factor EF-Tu. GTP complex stabilizes an orthoester acid intermediate structure of aminoacyl-tRNA in a ternary complex
12. Modification interference approach to detect ribose moieties important for the optimal activity of a ribozyme
13. Incorrect aminoacylations involving tRNAs or valyl-tRNA synthetase from Bacillus stearothermophilus
14. Calculation of protein extinction coefficients from amino acid sequence data
15. Rp-deoxy-phosphorothioate modification interference experiments identify 2′-OH groups in RNase P RNA that are crucial to tRNA binding
16. Isomeric aminoacyl-tRNAs are both bound by elongation factor Tu
17. Recognition of the high affinity binding site in rev-response element RNA by the human immunodeficiency virus type-1 rev protein
18. Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu. GTP: Evidence for a new functional role for elongation factor Tu in protein biosynthesis
19. 2+ in 15-year old crystals
20. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
21. Discrimination between aminoacyl groups on su+ 7 tRNA by elongation factor Tu
22. Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP
23. Elongation factor Tu and the aminoacyl-tRNA-EFTu-GTP complex
24. Defining a smaller RNA substrate for elongation factor Tu
25. Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation
26. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog
27. The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA
28. Ternary complexes of Escherichia coli aminoacyl-tRNAs with the elongation factor Tu and GTP: Thermodynamic and structural studies
29. Mapping contacts between Escherichia coli alanyl tRNA synthetase and 2′ hydroxyls using a complete tRNA molecule
30. GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs
31. Transient conformational states of aminoacyl-tRNA during ribosome binding catalyzed by elongation factor Tu
32. Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu
33. Nucleotide analog interference mapping of the hairpin ribozyme: Implications for secondary and tertiary structure formation
34. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
35. Role of the tertiary nucleotides in the interaction of yeast phenylalanine tRNA with its cognate synthetase
36. Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase
37. The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: A classic structure revisited
38. Role of the 5′-terminal phosphate of tRNA for its function during protein biosynthesis elongation cycle
39. Crystal structure of yeast phenylalanine transfer RNA. I. Crystallographic refinement
40. Aminoacyl-tRNA exclusively in the 3′-isomeric form is bound to polypeptide chain elongation factor Tu
41. Asp: A nucleotide analogue interference study
42. The complex formation between Escherichia coli aminoacyl-tRNA, elongation factor Tu and GTP. The effect of the side-chain of the amino acid linked to tRNA
43. Activity of the 2′ and 3′ isomers of aminoacyl transfer ribonucleic acid in the in vitro peptide elongation on Escherichia coli ribosomes
44. A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions
45. Transfer RNA aminoacylation: Identification of a critical ribose 2′-hydroxyl-base interaction