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Upstream regulatory sequences from two β-conglycinin genes

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Abstract

Genes encoding the β-conglycinin seed storage proteins of soybean are expressed only in seeds during specific stages of development. The different subunits of β-conglycinin, α′, α and β, are encoded by distinct members of a gene family. Yet there are marked differences in the regulation of the genes encoding the α′/α and β subunits. Previous work (Chen et al., EMBO J 7: 297–302, 1988) identified a seed specific transcriptional enhancer upstream of a gene encoding the α′ subunit. Mutations were made within this region to discern its functional components. Among those identified is a 62 bp region (between −77 and −140) that contains a vicilin box consensus sequence as well as a sequence that binds the soybean nuclear factor SEF4 in vitro. A second region, which contains a sequence homologous to the core of the legumin box consensus (i.e., CATGCAT-like or RY repeat element) at −246, was also shown to affect the activity of this enhancer in transgenic plants. A series of 5′ terminal deletions were used to identify regulatory elements upstream of the β subunit gene. Two regions were identified (from −553 to −442 and from −308 to −72) that, when deleted, led to a marked reduction in gene expression. Both of these elements contain sequences that bind SEF4 in vitro. The distal element also contains an AT-rich segment that recognizes a second nuclear factor, SEF1, in vitro. Neither of these elements contains any homology to the vicilin box consensus.

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References

  1. Allen RD, Bernier F, Lessard PA, Beachy RN: Nuclear factors interact with a soybean β-conglycinin enhancer. Plant Cell 1: 623–631 (1989).

    PubMed  Google Scholar 

  2. Barker SJ, Goldberg RB: β-conglycinin gene sequences differentially program tobacco endosperm and embryo expression patterns. J Cell Biochem, Suppl 15A: 87 (1991).

  3. Barker SJ, Harada JJ, Goldberg RB: Cellular localization of soybean storage protein mRNA in transformed tobacco seeds. Proc Natl Acad Sci USA 85: 458–462 (1988).

    Google Scholar 

  4. Beachy RN, Chen Z-L, Horsch RB, Rogers SG, Hoffmann NL, Fraley RT: Accumulation and assembly of soybean β-conglycinin in seeds of transformed petunia plants. EMBO J 4: 3047–3053 (1985).

    Google Scholar 

  5. Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254 (1976).

    Article  PubMed  Google Scholar 

  6. Bray EA, Beachy RN: Regulation by ABA of β-conglycinin expression in cultured developing soybean cotyledons. Plant Physiol 79: 746–750 (1985).

    Google Scholar 

  7. Bray EA, Naito S, Pan N-S, Anderson EA, Dubé P, Beachy RN: Expression of the β-subunit of β-conglycinin in seeds of transgenic plants. Planta 172: 364–370 (1987).

    Article  Google Scholar 

  8. Burow MD, Sen P, Chlan CA, Murai N: Developmental control of the β-phaseolin gene requires positive, negative, and temporal seed-specific regulatory elements and a negative element for stem and root expression. Plant J 2: 537–548 (1992).

    Google Scholar 

  9. Bustos MM, Begum D, Kalkan F, Battraw MJ, Hall TC: Positive and negative cis-acting DNA domains are required for spatial and temporal regulation of gene expression by a seed storage protein promoter. EMBO J 10: 1469–1479 (1991).

    PubMed  Google Scholar 

  10. Bustos MM, Guiltinan MJ, Jordano J, Begum F, Kalkan A, Hall TC: Regulation of β-glucuronidase expression in transgenic plants by an A/T rich cis acting sequence found upstream of a French bean β phaseolin gene. Plant Cell 1: 839–853 (1989).

    Article  PubMed  Google Scholar 

  11. Chamberland S, Daigle N, Bernier F: The legumin boxes and the 3′ part of a soybean β-conglycinin promoter are involved in seed gene expression in transgenic tobacco plants. Plant Mol Biol 19: 937–949 (1992).

    PubMed  Google Scholar 

  12. Chen Z-L, Pan N-S, Beachy RN: A DNA sequence element that confers seed-specific enhancement to a constitutive promoter. EMBO J 2: 297–302 (1988).

    Google Scholar 

  13. Chen Z-L, Schuler MA, Beachy RN: Functional analysis of regulatory elements in a plant embryo-specific gene. Proc Natl Acad Sci USA 83: 8560–8564 (1986).

    PubMed  Google Scholar 

  14. Doyle JJ, Schuler MA, Godette WD, Zenger V, Beachy RN, Slightom JL: The glycosylated seed storage proteins of Glycine max and Phaseolus vulgaris. Structural homologies of genes and proteins. J Biol Chem 261: 9928–9238 (1986).

    Google Scholar 

  15. Figuvski DH, Helinski DR: Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc Natl Acad Sci USA 76: 1648–1652 (1979).

    PubMed  Google Scholar 

  16. Fraley RT, Rogers SG, Horsch RB, Eicholtz DA, Flick JS, Fink CL, Hoffman NL, Sanders PR: The SEV system: a new disarmed Ti plasmid vector system for plant transformation. Bio/technology 3: 629–635 (1985).

    Article  Google Scholar 

  17. Fujiwara T, Hirai MY, Chino M, Komeda Y, Naito S: Effects of sulfur nutrition on expression of the soybean seed storage protein genes in transgenic petunia. Plant Physiol 99: 263–268 (1992).

    Google Scholar 

  18. Fujiwara T, Naito S, Chino M, Nagata T: Electroporated protoplasts express seed specific gene promoters. Plant Cell Rep 9: 602–606 (1991).

    Article  Google Scholar 

  19. Gatehouse JA, Evans IM, Croy RRD, Boulter D: Differential expression of genes during legume seed development. Phil Trans R Soc Lond B 314: 367–384 (1986).

    Google Scholar 

  20. Gilmartin PM, Sarokin L, Memelink J, Chua N-H: Molecular light switches for plant genes. Plant Cell 2: 369–378 (1990).

    Article  PubMed  Google Scholar 

  21. Goldberg RB, Hoschek G, Ditta GS, Briedenbach RW: Developmental regulation of cloned superabundant embryo mRNAs in soybean. Devel Biol 83: 218–231 (1981).

    Google Scholar 

  22. Grasser KD, Maier U-G, Haass MM, Feix G: Maize high mobility group proteins bind to CCAAT and TATA boxes of a zein gene promoter. J Biol Chem 265: 4185–4188 (1990).

    PubMed  Google Scholar 

  23. Harada JJ, Barker SJ, Goldberg RB: Soybean β-conglycinin genes are clustered in several DNA regions and are regulated by transcriptional and posttranscriptional processes. Plant Cell 1: 415–425 (1989).

    Article  PubMed  Google Scholar 

  24. Holowach LP, Madison JT, Thompson JF: Studies on the mechanism of regulation of the mRNA level for a soybean storage protein subunit by exogenous L-methionine. Plant Physiol 80: 561–567 (1986).

    Google Scholar 

  25. Holowach LP, Thompson JF, Madison JT: Effects of exogenous methionine on storage protein composition of soybean cotyledons cultured in vitro. Plant Physiol 74: 576–583 (1984).

    Google Scholar 

  26. Horsch RB, Fry JE, Hoffman NL, Eicholtz D, Rogers SG, Fraley RT: A simple and general method for transferring genes into plants. Science 227: 1229–1231 (1985).

    Google Scholar 

  27. Horsch RB, Klee HJ: Rapid assay of foreign gene expression in leaf discs transformed by Agrobacterium tumefaciens: Role of T-DNA borders in the transfer process. Proc Natl Acad Sci USA 83: 4428–4432 (1986).

    Google Scholar 

  28. Jefferson RA, Burgess SM, Hirsch D: β-glucuronidase from E. coli as a gene-fusion marker. Proc Natl Acad Sci USA 83: 8447–8451 (1986).

    PubMed  Google Scholar 

  29. Jefferson RA: Assaying chimeric genes in plants: the GUS gene fusion system. Plant Mol Biol Rep 5: 387–405 (1987).

    Google Scholar 

  30. Jefferson RA, Kavanagh TA, Bevan MW: GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J 6: 3901–3907 (1987).

    PubMed  Google Scholar 

  31. Jordano J, Concepción A, Thomas TL: A sunflower helianthinin gene upstream sequence ensemble contains an enhancer and sites of nuclear protein interaction. Plant Cell 1: 855–866 (1989).

    Article  PubMed  Google Scholar 

  32. Ladin BF, Tierney ML, Meinke DW, Hosángadi P, Vieth M, Beachy RN: Developmental regulation of β-conglycinin in soybean axes and cotyledons. Plant Physiol 84: 35–41 (1987).

    Google Scholar 

  33. Lessard PA, Allen RD, Bernier F, Crispino JD, Fujiwara T, Beachy RN: Multiple nuclear factors interact with upstream sequences of differentially regulated β-conglycinin genes. Plant Mol Biol 16: 397–413 (1991).

    Article  PubMed  Google Scholar 

  34. Meinke DW, Chen J, Beachy RN: Expression of storage-protein genes during soybean seed development. Planta 153: 130–139 (1981).

    Google Scholar 

  35. Naito S, Dubé PH, Beachy RN: Differential expression α′ and β subunit genes in transgenic plants. Plant Mol Biol 11: 109–123 (1988).

    Google Scholar 

  36. Shirsat AH: Control of gene expression in the developing seed. In: Grierson D (ed) Developmental Regulation of Plant Gene Expression, pp. 153–181. Chapman and Hall, New York (1991).

    Google Scholar 

  37. Siegel S, Castellan NJJr.: Nonparametric Statistics for the Behavioral Sciences. McGraw-Hill, New York (1988).

    Google Scholar 

  38. Ueda T, Pichersky E, Malik VS, Cashmore AR: Level of expression of the tomato rbcS-3A gene is modulated by a far upstream promoter element in a developmentally regulated manner. Plant Cell 1: 217–227 (1989).

    Article  PubMed  Google Scholar 

  39. Yanisch-Perron C, Vieira J, Messing J: Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33: 103–119 (1985).

    Article  PubMed  Google Scholar 

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Lessard, P.A., Allen, R.D., Fujiwara, T. et al. Upstream regulatory sequences from two β-conglycinin genes. Plant Mol Biol 22, 873–885 (1993). https://doi.org/10.1007/BF00027372

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