Regulation of the Utilization of MRNA for Eucaryotic Elongation Factor Tu in Friend Erythroleukemia Cells

Overview

Journal Mol Cell Biol

Specialty Cell Biology

Date 1987 Feb 1

PMID 2434834

Citations 7

Authors

T R Rao

L I SLOBIN

Affiliations

Soon will be listed here.

Abstract

When Friend erythroleukemia cells were allowed to grow to stationary phase (2 X 10(6) to 3 X 10(6) cells per ml), approximately 60% of the mRNA for eucaryotic elongation factor Tu (eEF-Tu) sedimented at less than or equal to 80S, and most of the remaining factor mRNA was associated with small polysomes. Under the same growth conditions, greater than 90% of the mRNA for eucaryotic initiation factor 4A remained associated with polysomes. The association of eEF-Tu mRNA with polysomes changed dramatically when stationary-phase cells were treated with fresh medium. After 1 h in fresh medium, approximately 90% of eEF-Tu mRNA in Friend cells was found in heavy polysomes. Associated with the shift of eEF-Tu mRNA into heavy polysomes, we found at least a 2.6-fold increase in the synthesis of eEF-Tu in vivo as well as a remarkable 40% decrease in the total amount of eEF-Tu mRNA per cell. Our data raise the possibility that eEF-Tu mRNA that has accumulated in ribonucleoprotein particles in stationary-phase cells is degraded rather than reutilized for eEF-Tu synthesis.

Citing Articles

Mechanisms of miRNA-Mediated Gene Regulation from Common Downregulation to mRNA-Specific Upregulation.

Orang A, Safaralizadeh R, Kazemzadeh-Bavili M Int J Genomics. 2014; 2014:970607.

PMID: 25180174 PMC: 4142390. DOI: 10.1155/2014/970607.

Coordinate translational regulation in the syntheses of elongation factor 1 alpha and ribosomal proteins in Xenopus laevis.

Loreni F, Francesconi A, Amaldi F Nucleic Acids Res. 1993; 21(20):4721-5.

PMID: 8233819 PMC: 331496. DOI: 10.1093/nar/21.20.4721.

Vertebrate mRNAs with a 5'-terminal pyrimidine tract are candidates for translational repression in quiescent cells: characterization of the translational cis-regulatory element.

Avni D, Shama S, Loreni F, Meyuhas O Mol Cell Biol. 1994; 14(6):3822-33.

PMID: 8196625 PMC: 358749. DOI: 10.1128/mcb.14.6.3822-3833.1994.

Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins.

Terada N, Patel H, Takase K, Kohno K, Nairn A, Gelfand E Proc Natl Acad Sci U S A. 1994; 91(24):11477-81.

PMID: 7972087 PMC: 45254. DOI: 10.1073/pnas.91.24.11477.

Peptide-chain elongation in eukaryotes.

Proud C Mol Biol Rep. 1994; 19(3):161-70.

PMID: 7969104 DOI: 10.1007/BF00986958.

References

Preobrazhensky A, Spirin A . Informosomes and their protein components: the present state of knowledge. Prog Nucleic Acid Res Mol Biol. 1978; 21:1-38. DOI: 10.1016/s0079-6603(08)60265-2. View

Lodish H . Alpha and beta globin messenger ribonucleic acid. Different amounts and rates of initiation of translation. J Biol Chem. 1971; 246(23):7131-8. View

Thomas G, Luther H . Transcriptional and translational control of cytoplasmic proteins after serum stimulation of quiescent Swiss 3T3 cells. Proc Natl Acad Sci U S A. 1981; 78(9):5712-6. PMC: 348838. DOI: 10.1073/pnas.78.9.5712. View

Duncan R, Hershey J . Regulation of initiation factors during translational repression caused by serum depletion. Abundance, synthesis, and turnover rates. J Biol Chem. 1985; 260(9):5486-92. View

SLOBIN L, Jordan P . Translational repression of mRNA for eucaryotic elongation factors in Friend erythroleukemia cells. Eur J Biochem. 1984; 145(1):143-50. DOI: 10.1111/j.1432-1033.1984.tb08533.x. View

Kozak M . Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 1984; 12(2):857-72. PMC: 318541. DOI: 10.1093/nar/12.2.857. View

Ray A, Walden W, Brendler T, Zenger V, Thach R . Effect of medium hypertonicity on reovirus translation rates. An application of kinetic modeling in vivo. Biochemistry. 1985; 24(26):7525-32. DOI: 10.1021/bi00347a004. View

Cheley S, Anderson R . A reproducible microanalytical method for the detection of specific RNA sequences by dot-blot hybridization. Anal Biochem. 1984; 137(1):15-9. DOI: 10.1016/0003-2697(84)90339-7. View

Kay M, Jacobs-Lorena M . Selective translational regulation of ribosomal protein gene expression during early development of Drosophila melanogaster. Mol Cell Biol. 1985; 5(12):3583-92. PMC: 369189. DOI: 10.1128/mcb.5.12.3583-3592.1985. View

10.

Rao T, SLOBIN L . Structure of the amino-terminal end of mammalian elongation factor Tu. Nucleic Acids Res. 1986; 14(5):2409. PMC: 339668. DOI: 10.1093/nar/14.5.2409. View

11.

Pelletier J, Sonenberg N . Insertion mutagenesis to increase secondary structure within the 5' noncoding region of a eukaryotic mRNA reduces translational efficiency. Cell. 1985; 40(3):515-26. DOI: 10.1016/0092-8674(85)90200-4. View

12.

Geoghegan T, Cereghini S, Brawerman G . Inactive mRNA-protein complexes from mouse sarcoma-180 ascites cells. Proc Natl Acad Sci U S A. 1979; 76(11):5587-91. PMC: 411694. DOI: 10.1073/pnas.76.11.5587. View

13.

INFANTE A, Heilmann L . Distribution of messenger ribonucleic acid in polysomes and nonpolysomal particles of sea urchin embryos: translational control of actin synthesis. Biochemistry. 1981; 20(1):1-8. DOI: 10.1021/bi00504a001. View

14.

Mauron A, Spohr G . Kinetics of synthesis of cytoplasmic messenger-like RNA not associated with ribosomes in HeLa cells. Eur J Biochem. 1978; 82(2):619-25. DOI: 10.1111/j.1432-1033.1978.tb12058.x. View

15.

Nielsen P, McMaster G, Trachsel H . Cloning of eukaryotic protein synthesis initiation factor genes: isolation and characterization of cDNA clones encoding factor eIF-4A. Nucleic Acids Res. 1985; 13(19):6867-80. PMC: 322010. DOI: 10.1093/nar/13.19.6867. View

16.

Brands J, Maassen J, van Hemert F, Amons R, Moller W . The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites. Eur J Biochem. 1986; 155(1):167-71. DOI: 10.1111/j.1432-1033.1986.tb09472.x. View

17.

Dean M, Levine R, Ran W, Kindy M, Sonenshein G, Campisi J . Regulation of c-myc transcription and mRNA abundance by serum growth factors and cell contact. J Biol Chem. 1986; 261(20):9161-6. View

18.

Singh L, Jones K . The use of heparin as a simple cost-effective means of controlling background in nucleic acid hybridization procedures. Nucleic Acids Res. 1984; 12(14):5627-38. PMC: 320019. DOI: 10.1093/nar/12.14.5627. View

19.

Bienz M, Gurdon J . The heat-shock response in Xenopus oocytes is controlled at the translational level. Cell. 1982; 29(3):811-9. DOI: 10.1016/0092-8674(82)90443-3. View

20.

Nielsen P, McConkey E . Evidence for control of protein synthesis in HeLa cells via the elongation rate. J Cell Physiol. 1980; 104(3):269-81. DOI: 10.1002/jcp.1041040302. View