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Eur J Biochem. 1996 Mar 1;236(2):383-8.

The translational cis-regulatory element of mammalian ribosomal protein mRNAs is recognized by the plant translational apparatus.

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Department of Developmental Biochemistry, Institute of Biochemistry, The Hebrew University-Hadassah Medical School, Jerusalem, Israel.


The translational efficiency of mammalian ribosomal protein mRNAs correlates with the growth status of the cells and its control is mediated through a 5' terminal oligopyrimidine tract (5' TOP) common to all these mRNAs. In the present study, we demonstrate that the plant translational apparatus, as represented by wheat-germ extract, discriminates against mammalian mRNAs containing this motif to the same extent as do quiescent mammalian cells. Moreover, mutations in the 5' TOP, which abolish the growth-dependent translational control of the respective mRNAs in mammalian cells, render these mRNAs refractory to discrimination in the plant cell-free system. This selective discrimination reflects neither the specific instability of 5' TOP-containing mRNAs during the incubation in vitro nor a lower competitive potential for the cap-binding protein. The lower in vitro translational efficiency of these mRNAs is an inherent feature which is independent of whether they were derived from polysomes or messenger ribonucleoprotein particles of the transfected mammalian cells. The conservation of the discriminatory property of the translational apparatus between the animal and plant kingdoms is discussed from mechanistic and evolutionary points of view.

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