The fMet-tRNA binding domain of translational initiation factor IF2: role and environment of its two Cys residues

Item Type:	Article
Title:	The fMet-tRNA binding domain of translational initiation factor IF2: role and environment of its two Cys residues
Creators Name:	Misselwitz, R. and Welfle, K. and Krafft, C. and Welfle, H. and Brandi, L. and Caserta, E. and Gualerzi, C.O.
Abstract:	Mutations of the cysteines (positions 668 and 714) were generated in the IF2 C domain of Bacillus stearothermophilus translation initiation factor IF2. The corresponding proteins were characterized functionally and structurally. Most (yet not all) amino acid replacements at both positions resulted in severe reduction of the fMet-tRNA binding activity of IF2 C without grossly altering its structure. Our work demonstrates that: (a) both Cys residues are buried within an hydrophobic core and not accessible to protonation or chemical substitution, (b) neither Cys is functionally essential and (c) both Cys residues are located near the active site, probably without participating directly in fMet-tRNA binding.
Keywords:	Protein Synthesis, fMet-tRNA Binding, Protein Domain, Site-Directed Mutagenesis, Protein Unfolding, Raman Spectroscopy
Source:	FEBS Letters
ISSN:	0014-5793
Publisher:	Elsevier
Volume:	459
Number:	3
Page Range:	332-336
Date:	15 October 1999
Official Publication:	https://doi.org/10.1016/S0014-5793(99)01280-6
PubMed:	View item in PubMed

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