PMID: 3513840Mar 26, 1986

Formylmethionyl-tRNA binding to 30 S ribosomes programmed with homopolynucleotides and the effect of translational initiation factor 3

Biochimica Et Biophysica Acta
B BerkhoutP Van Knippenberg


Binding of the polynucleotides poly(U), poly(X) and poly(dT) to 30 S ribosomes of Escherichia coli triggers IF2-dependent binding of initiator-tRNA (fMet-tRNA) to these particles. Poly(A) and poly(C) are inactive. A minimum chain-length of approximately 100 residues in poly(U) is required for full activity in fMet-tRNA binding, although much shorter polymers bind tightly to 30 S particles and do stimulate the binding of acPhe-tRNA. The stimulation of fMet-tRNA binding to 30 S ribosomes is strongly reduced under conditions where the polynucleotides adopt secondary structure. Complexes containing fMet-tRNA and the non-cognate codon UUU or XXX are destabilized by IF3, whereas the formation of such a complex containing an AUG codon is slightly enhanced by the factor. Consistent with previous observations, it was found that all model initiation complexes containing acPhe-tRNA are strongly destabilized by IF3, even when the cognate codon (UUU) is present. Our results suggest that IF3 counteracts 'unnatural' initiation events in vitro and suggest a regulatory role for this factor in vivo.


Apr 14, 1999·Proceedings of the National Academy of Sciences of the United States of America·J P McCutcheonJ Frank
Jul 25, 1989·Nucleic Acids Research·R A Spanjaard, J van Duin
Jul 1, 1989·Molecular & General Genetics : MGG·M R Adhin, J van Duin
May 18, 1999·Journal of Molecular Biology·C SacerdotM Springer
Mar 5, 1991·Journal of Molecular Biology·D HartzL Gold
Jan 15, 1997·European Journal of Biochemistry·H P VornlocherM Sprinzl
Mar 28, 1998·The Journal of Biological Chemistry·N J Yu, Linda L Spremulli

Related Concepts

poly(xanthylic acid)
tRNA, formylmethionine-
Sense Codon
Alkalescens-Dispar Group
RNA Conformation
Peptide Initiation Factors
Poly T
Poly U

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