Abstract
The secondary structure of zein mRNA affects its translational potential. Here we show that in a cell-free system the translation efficiency of zein mRNA containing inverted repeats in the 5'- and 3'-untranslated regions is reduced. This translational block is released after deletion of the 3'-inverted repeat. We conclude that the translational block is caused by hybrid formation between the two inverted repeats. The translational efficiency of zein mRNAs, is also affected by varying the length or the primary structure of the 5'-untranslated region.
Keywords: in vitro transcription-translation, zein mRNA, inverted repeats, 5'- and 3'-untranslated regions, translational potential
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- Anderson O. D., Litts J. C., Gautier M. F., Greene F. C. Nucleic acid sequence and chromosome assignment of a wheat storage protein gene. Nucleic Acids Res. 1984 Nov 12;12(21):8129–8144. doi: 10.1093/nar/12.21.8129. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Berkner K. L., Sharp P. A. Effect of the tripartite leader on synthesis of a non-viral protein in an adenovirus 5 recombinant. Nucleic Acids Res. 1985 Feb 11;13(3):841–857. doi: 10.1093/nar/13.3.841. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gheysen D., Iserentant D., Derom C., Fiers W. Systematic alteration of the nucleotide sequence preceding the translation initiation codon and the effects on bacterial expression of the cloned SV40 small-t antigen gene. Gene. 1982 Jan;17(1):55–63. doi: 10.1016/0378-1119(82)90100-7. [DOI] [PubMed] [Google Scholar]
- Gold L., Pribnow D., Schneider T., Shinedling S., Singer B. S., Stormo G. Translational initiation in prokaryotes. Annu Rev Microbiol. 1981;35:365–403. doi: 10.1146/annurev.mi.35.100181.002053. [DOI] [PubMed] [Google Scholar]
- Gordon G., Gayda R. C., Markovitz A. Sequence of the regulatory region of omp T, the gene specifying major outer membrane protein a (3b) of Escherichia coli K-12: implications for regulation and processing. Mol Gen Genet. 1984;193(3):414–421. doi: 10.1007/BF00382077. [DOI] [PubMed] [Google Scholar]
- Gough N. M., Metcalf D., Gough J., Grail D., Dunn A. R. Structure and expression of the mRNA for murine granulocyte-macrophage colony stimulating factor. EMBO J. 1985 Mar;4(3):645–653. doi: 10.1002/j.1460-2075.1985.tb03678.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hall M. N., Gabay J., Débarbouillé M., Schwartz M. A role for mRNA secondary structure in the control of translation initiation. Nature. 1982 Feb 18;295(5850):616–618. doi: 10.1038/295616a0. [DOI] [PubMed] [Google Scholar]
- Horinouchi S., Weisblum B. Posttranscriptional modification of mRNA conformation: mechanism that regulates erythromycin-induced resistance. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7079–7083. doi: 10.1073/pnas.77.12.7079. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hu N. T., Peifer M. A., Heidecker G., Messing J., Rubenstein I. Primary structure of a genomic zein sequence of maize. EMBO J. 1982;1(11):1337–1342. doi: 10.1002/j.1460-2075.1982.tb01319.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hurt E. C., Pesold-Hurt B., Schatz G. The amino-terminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix. EMBO J. 1984 Dec 20;3(13):3149–3156. doi: 10.1002/j.1460-2075.1984.tb02272.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kaufman R. J., Sharp P. A. Construction of a modular dihydrofolate reductase cDNA gene: analysis of signals utilized for efficient expression. Mol Cell Biol. 1982 Nov;2(11):1304–1319. doi: 10.1128/mcb.2.11.1304. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kozak M. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev. 1983 Mar;47(1):1–45. doi: 10.1128/mr.47.1.1-45.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kozak M. Influence of mRNA secondary structure on binding and migration of 40S ribosomal subunits. Cell. 1980 Jan;19(1):79–90. doi: 10.1016/0092-8674(80)90390-6. [DOI] [PubMed] [Google Scholar]
- Kridl J. C., Vieira J., Rubenstein I., Messing J. Nucleotide sequence analysis of a zein genomic clone with a short open reading frame. Gene. 1984 Apr;28(1):113–118. doi: 10.1016/0378-1119(84)90093-3. [DOI] [PubMed] [Google Scholar]
- Larkins B. A., Pedersen K., Handa A. K., Hurkman W. J., Smith L. D. Synthesis and processing of maize storage proteins in Xenopus laevis oocytes. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6448–6452. doi: 10.1073/pnas.76.12.6448. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Logan J., Shenk T. Adenovirus tripartite leader sequence enhances translation of mRNAs late after infection. Proc Natl Acad Sci U S A. 1984 Jun;81(12):3655–3659. doi: 10.1073/pnas.81.12.3655. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Martin S. L., Zimmer E. A., Davidson W. S., Wilson A. C., Kan Y. W. The untranslated regions of beta-globin mRNA evolve at a functional rate in higher primates. Cell. 1981 Sep;25(3):737–741. doi: 10.1016/0092-8674(81)90181-1. [DOI] [PubMed] [Google Scholar]
- Mignery G. A., Pikaard C. S., Hannapel D. J., Park W. D. Isolation and sequence analysis of cDNAs for the major potato tuber protein, patatin. Nucleic Acids Res. 1984 Nov 12;12(21):7987–8000. doi: 10.1093/nar/12.21.7987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miyata T., Yasunaga T., Nishida T. Nucleotide sequence divergence and functional constraint in mRNA evolution. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7328–7332. doi: 10.1073/pnas.77.12.7328. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pavlakis G. N., Lockard R. E., Vamvakopoulos N., Rieser L., RajBhandary U. L., Vournakis J. N. Secondary structure of mouse and rabbit alpha- and beta-globin mRNAs: differential accessibility of alpha and beta initiator AUG codons towards nucleases. Cell. 1980 Jan;19(1):91–102. doi: 10.1016/0092-8674(80)90391-8. [DOI] [PubMed] [Google Scholar]
- Pedersen K., Devereux J., Wilson D. R., Sheldon E., Larkins B. A. Cloning and sequence analysis reveal structural variation among related zein genes in maize. Cell. 1982 Jul;29(3):1015–1026. doi: 10.1016/0092-8674(82)90465-2. [DOI] [PubMed] [Google Scholar]
- Pelletier J., Sonenberg N. Insertion mutagenesis to increase secondary structure within the 5' noncoding region of a eukaryotic mRNA reduces translational efficiency. Cell. 1985 Mar;40(3):515–526. doi: 10.1016/0092-8674(85)90200-4. [DOI] [PubMed] [Google Scholar]
- Radloff R., Bauer W., Vinograd J. A dye-buoyant-density method for the detection and isolation of closed circular duplex DNA: the closed circular DNA in HeLa cells. Proc Natl Acad Sci U S A. 1967 May;57(5):1514–1521. doi: 10.1073/pnas.57.5.1514. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosenberg M., Paterson B. M. Efficient cap-dependent translation of polycistronic prokaryotic mRNAs is restricted to the first gene in the operon. Nature. 1979 Jun 21;279(5715):696–701. doi: 10.1038/279696a0. [DOI] [PubMed] [Google Scholar]
- Salser W. Globin mRNA sequences: analysis of base pairing and evolutionary implications. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 2):985–1002. doi: 10.1101/sqb.1978.042.01.099. [DOI] [PubMed] [Google Scholar]
- Shah D. M., Hightower R. C., Meagher R. B. Complete nucleotide sequence of a soybean actin gene. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1022–1026. doi: 10.1073/pnas.79.4.1022. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Slightom J. L., Sun S. M., Hall T. C. Complete nucleotide sequence of a French bean storage protein gene: Phaseolin. Proc Natl Acad Sci U S A. 1983 Apr;80(7):1897–1901. doi: 10.1073/pnas.80.7.1897. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spena A., Viotti A., Pirrotta V. A homologous repetitive block structure underlies the heterogeneity of heavy and light chain zein genes. EMBO J. 1982;1(12):1589–1594. doi: 10.1002/j.1460-2075.1982.tb01360.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spena A., Viotti A., Pirrotta V. Two adjacent genomic zein sequences: structure, organization and tissue-specific restriction pattern. J Mol Biol. 1983 Oct 5;169(4):799–811. doi: 10.1016/s0022-2836(83)80137-5. [DOI] [PubMed] [Google Scholar]
- Stueber D., Ibrahimi I., Cutler D., Dobberstein B., Bujard H. A novel in vitro transcription-translation system: accurate and efficient synthesis of single proteins from cloned DNA sequences. EMBO J. 1984 Dec 20;3(13):3143–3148. doi: 10.1002/j.1460-2075.1984.tb02271.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tabata T., Sasaki K., Iwabuchi M. The structural organization and DNA sequence of a wheat histone H4 gene. Nucleic Acids Res. 1983 Sep 10;11(17):5865–5875. doi: 10.1093/nar/11.17.5865. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tessier L. H., Sondermeyer P., Faure T., Dreyer D., Benavente A., Villeval D., Courtney M., Lecocq J. P. The influence of mRNA primary and secondary structure on human IFN-gamma gene expression in E. coli. Nucleic Acids Res. 1984 Oct 25;12(20):7663–7675. doi: 10.1093/nar/12.20.7663. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thummel C., Tjian R., Hu S. L., Grodzicker T. Translational control of SV40 T antigen expressed from the adenovirus late promoter. Cell. 1983 Jun;33(2):455–464. doi: 10.1016/0092-8674(83)90427-0. [DOI] [PubMed] [Google Scholar]
- Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982 Oct;19(3):259–268. doi: 10.1016/0378-1119(82)90015-4. [DOI] [PubMed] [Google Scholar]
- Viotti A., Abildsten D., Pogna N., Sala E., Pirrotta V. Multiplicity and diversity of cloned zein cDNA sequences and their chromosomal localisation. EMBO J. 1982;1(1):53–58. doi: 10.1002/j.1460-2075.1982.tb01123.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zaret K. S., Sherman F. DNA sequence required for efficient transcription termination in yeast. Cell. 1982 Mar;28(3):563–573. doi: 10.1016/0092-8674(82)90211-2. [DOI] [PubMed] [Google Scholar]
- von Loringhoven A. F., Koch S., Hofschneider P. H., Koshy R. Co-transcribed 3' host sequences augment expression of integrated hepatitis B virus DNA. EMBO J. 1985 Jan;4(1):249–255. doi: 10.1002/j.1460-2075.1985.tb02343.x. [DOI] [PMC free article] [PubMed] [Google Scholar]