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The 5' Terminal Oligopyrimidine Tract Confers Translational Control on TOP MRNAs in a Cell Type- and Sequence Context-dependent Manner

Overview
Specialty Biochemistry
Date 1997 Mar 1
PMID 9023110
Citations 61
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Abstract

TOP mRNAs are vertebrate transcripts which contain a 5'terminal oligopyrimidine tract (5'TOP), encode for ribosomal proteins and elongation factors 1alpha and 2, and are candidates for growth-dependent translational control mediated through their 5'TOP. In the present study we show that elongation factor 2 (EF2) mRNA is translationally regulated in a growth-dependent manner in cells of hematopoietic origin, but not in any of three different non-hematopoietic cell lines studied. Human beta1-tubulin mRNA is a new member of the family which contains all the hallmarks of a typical TOP mRNA, yet its translation is refractory to growth arrest of any of the examined cell lines. Transfection experiments indicate that the first 29 and 53 nucleotides of the mRNAs encoding EF2 and beta1-tubulin, respectively, contain all the translational cis-regulatory elements sufficient for ubiquitously conferring growth-dependent translational control on a reporter mRNA. These results suggest that the distinct translational regulation of TOP mRNAs reflects downstream sequences which can override the regulatory features of the 5'TOP in a cell type-specific manner. This notion is further supported by the fact that mutations within the region immediately downstream of the 5'TOP of rpS16 mRNA confer onto the resulting transcripts growth-dependent translational control with a cell type specificity similar to that displayed by EF2 mRNA.

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References
1.
Lewis S, Gilmartin M, Hall J, Cowan N . Three expressed sequences within the human beta-tubulin multigene family each define a distinct isotype. J Mol Biol. 1985; 182(1):11-20. DOI: 10.1016/0022-2836(85)90023-3. View

2.
Wiedemann L, PERRY R . Characterization of the expressed gene and several processed pseudogenes for the mouse ribosomal protein L30 gene family. Mol Cell Biol. 1984; 4(11):2518-28. PMC: 369083. DOI: 10.1128/mcb.4.11.2518-2528.1984. View

3.
Selden R, Howie K, Rowe M, Goodman H, Moore D . Human growth hormone as a reporter gene in regulation studies employing transient gene expression. Mol Cell Biol. 1986; 6(9):3173-9. PMC: 367053. DOI: 10.1128/mcb.6.9.3173-3179.1986. View

4.
Chan Y, Lin A, McNally J, Wool I . The primary structure of rat ribosomal protein L5. A comparison of the sequence of amino acids in the proteins that interact with 5 S rRNA. J Biol Chem. 1987; 262(26):12879-86. View

5.
Meyuhas O, Thompson Jr E, PERRY R . Glucocorticoids selectively inhibit translation of ribosomal protein mRNAs in P1798 lymphosarcoma cells. Mol Cell Biol. 1987; 7(8):2691-9. PMC: 367885. DOI: 10.1128/mcb.7.8.2691-2699.1987. View