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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Misselwitz R,Welfle K,Krafft C,Welfle H,Brandi L,Caserta E,Gualerzi COdoi
10.1016/s0014-5793(99)01280-6keywords:
subject
Has Abstractpub_date
1999-10-15 00:00:00pages
332-6issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01280-6journal_volume
459pub_type
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