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Papers In Press, published online ahead of print February 19, 2002
Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899
Corresponding Author: Shatsky{at}libro.genebee.msu.su
p50, the major core protein bound to mammalian mRNAs, has been reported to stimulate translation at low p50/mRNA ratios and inhibit translation at high p50/mRNA ratios. This study aims to address the molecular mechanisms underlying these phenomena using the in vitro assembly of 48S preinitiation complexes from fully purified translational components in the presence or absence of p50 as analyzed by the toe-print assay. With limited concentrations of eIF2, eIF3, and eIF4F, p50 (but not PTB which was taken for comparison) strongly stimulates formation of the 48S preinitiation complexes with
J. Biol. Chem, 10.1074/jbc.M111954200
Submitted on December 14, 2001
Revised on February 13, 2002
Accepted on February 17, 2002
Positive and negative effects of the major mammalian mRNP protein p50 on binding of 40S ribosomal subunits to the initiation codon of beta -globin mRNA
-globin mRNA. This stimulation is observed when just a few molecules of p50 are bound per molecule of the mRNA. When the amount of p50 in solution is increased over some threshold p50/mRNA ratio, a remarkable repression is observed that can still be relieved by adding more eIF2 and eIF4F. At even higher concentrations of p50, the inhibitory effect becomes irreversible. The threshold ratio depends upon the extent of secondary structure of the 5'-untranslated region linked to the -globin coding region. Chemical probing has confirmed that the binding of p50 to mRNA involves only the sugar-phosphate backbone of the mRNA leaving nucleotide bases free for interaction with other mRNP components. These data are best compatible with the functional role of p50 as a "manager" of mRNA-protein interactions in mammalian mRNPs.
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