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

FEBS Letters

Krafft, Christoph²  Behlke, Joachim²  Heinemann, Udo²  Laettig, Stefan²  Welfle, Heinz²  Gualerzi, Claudio O.¹  Pon, Cynthia L.¹  Diehl, Annette² 

[1] Laboratory of Genetics, Department of Biology MCA, University of Camerino, 62032 Camerino (MC), Italy;Max-Delbrück-Centrum für Molekulare Medizin, D-13092 Berlin, Germany

关键词: Protein synthesis;    fMet-tRNA binding;    Analytical ultracentrifugation;    Raman spectroscopy;   

DOI  :  10.1016/S0014-5793(00)01377-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 μM, 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.

【 授权许可】

Unknown