Interaction of fMet-tRNAfMet with the C-terminal domain of translational initiation factor IF2 from Bacillus stearothermophilus

Item Type:	Article
Title:	Interaction of fMet-tRNAfMet with the C-terminal domain of translational initiation factor IF2 from Bacillus stearothermophilus
Creators Name:	Krafft, C. and Diehl, A. and Laettig, S. and Behlke, J. and Heinemann, U. and Pon, C.L. and Gualerzi, C.O. and Welfle, H.
Abstract:	Analytical ultracentrifugation studies indicated that the C-terminal domains of IF2 comprising amino acid residues 520-741 (IF2 C) and 632-741 (IF2 C-2) bind fMet-tRNA with similar affinities (K(d) at 25°C equal to 0.27 and 0.23 {mu}M, respectively). Complex formation between fMet-tRNA(fMet) and IF2 C or IF2 C-2 is accompanied by barely detectable spectral changes as demonstrated by a comparison of the Raman spectra of the complexes with the calculated sum of the spectra of the individual components. These results and the temperature dependence of the K(d) of the protein-RNA complexes indicate that complex formation is not accompanied by obvious conformational changes of the components, and possibly depends on a rather small binding site comprising only a few interacting residues of both components.
Keywords:	Analytical Ultracentrifugation, FMet-tRNA Binding, Protein Synthesis, Raman Spectroscopy
Source:	FEBS Letters
ISSN:	0014-5793
Publisher:	Elsevier
Volume:	471
Number:	2-3
Page Range:	128-132
Date:	14 April 2000
Official Publication:	https://doi.org/10.1016/S0014-5793(00)01377-6
PubMed:	View item in PubMed

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