PMID:9054966
| Citation |
Moreau, M, de Cock, E, Fortier, PL, Garcia, C, Albaret, C, Blanquet, S, Lallemand, JY and Dardel, F (1997) Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. J. Mol. Biol. 266:15-22 |
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| Abstract |
Initiation factor IF3 from Escherichia coli plays a critical role in the selection of the correct initiation codon. This protein is composed of two domains, connected by a lysin-rich hydrophilic linker. The conformation of native IF3 was investigated by heteronuclear NMR spectroscopy. The two domains are independent and show little or no interaction. Heteronuclear relaxation studies of a sample selectively labelled on lysine residues demonstrates that the inter-domain linker is highly flexible, exhibiting increased 15N T2 values and negative 1H[15N] nuclear Overhause effects over a length of at least eight residues. Analysis of the rotational correlation times further shows that the motions of the two domains are most likely uncorrelated. The inter-domain linker thus displays almost totally unrestricted motions. Accordingly, the amide protons in the central region are shown to be in fast exchange with water. Such a high degree of flexibility of the inter-domain linker might be required for IF3 domains to interact with distant regions of the ribosome. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Computer Simulation; Escherichia coli/metabolism; Magnetic Resonance Spectroscopy/methods; Models, Structural; Nitrogen Isotopes; Peptide Initiation Factors/chemistry; Peptide Initiation Factors/metabolism; Prokaryotic Initiation Factor-3; Protein Conformation; Ribosomes/metabolism; Solutions |
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