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. 1995 May;108(1):129–139. doi: 10.1104/pp.108.1.129

Characterization of nuclear factors for elicitor-mediated activation of the promoter of the pea phenylalanine ammonia-lyase gene 1.

H Kato 1, M Wada 1, K Muraya 1, K Malik 1, T Shiraishi 1, Y Ichinose 1, T Yamada 1
PMCID: PMC157313  PMID: 7540308

Abstract

The nuclear factors presumably associated with the activation of the gene encoding phenylalanine ammonia-lyase by a fungal elicitor were characterized in pea (Pisum sativum L.) epicotyls. The TATA-proximal region was dissected and putative cis-regulatory elements in the promoter of pea phenylalanine ammonia-lyase gene 1 were examined by gel-mobility shift and in vitro footprinting analyses. Specific binding of the nuclear factors to the promoter-proximal regions of pea phenylalanine ammonia-lyase gene 1 associated with elicitor-mediated activation was detected at a region containing consensus sequence motifs of boxes 2 and 4 and other AT-rich sequences. The analyses of DNA fragments containing the deleted promoter regions suggested that a residue from -183 to -173 (ATTAGTAAGTGAT) was essential for a maximal activity of forming low-mobility complex (LMC) in the gel-mobility shift assay, and synthetic oligonucleotides confirmed the presence of at least one nuclear component associated with the formation of an active LMC. Competition experiments and treatment with Hoechst 33258 provided direct evidence that the formation of LMC with the promoter fragments from genes encoding phenylalanine ammonia-lyase and chalcone synthase in pea contained one or more of the same proteins that recognize AT-rich sequence motifs for binding. It also suggests that common high-mobility group-like proteins might be involved in the regulation of elicitor-inducible genes in pea.

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Selected References

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  1. An C., Ichinose Y., Yamada T., Tanaka Y., Shiraishi T., Oku H. Organization of the genes encoding chalcone synthase in Pisum sativum. Plant Mol Biol. 1993 Mar;21(5):789–803. doi: 10.1007/BF00027112. [DOI] [PubMed] [Google Scholar]
  2. Datta N., Cashmore A. R. Binding of a pea nuclear protein to promoters of certain photoregulated genes is modulated by phosphorylation. Plant Cell. 1989 Nov;1(11):1069–1077. doi: 10.1105/tpc.1.11.1069. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dron M., Clouse S. D., Dixon R. A., Lawton M. A., Lamb C. J. Glutathione and fungal elicitor regulation of a plant defense gene promoter in electroporated protoplasts. Proc Natl Acad Sci U S A. 1988 Sep;85(18):6738–6742. doi: 10.1073/pnas.85.18.6738. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Du W., Thanos D., Maniatis T. Mechanisms of transcriptional synergism between distinct virus-inducible enhancer elements. Cell. 1993 Sep 10;74(5):887–898. doi: 10.1016/0092-8674(93)90468-6. [DOI] [PubMed] [Google Scholar]
  5. Giese K., Cox J., Grosschedl R. The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures. Cell. 1992 Apr 3;69(1):185–195. doi: 10.1016/0092-8674(92)90129-z. [DOI] [PubMed] [Google Scholar]
  6. Harrison M. J., Lawton M. A., Lamb C. J., Dixon R. A. Characterization of a nuclear protein that binds to three elements within the silencer region of a bean chalcone synthase gene promoter. Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2515–2519. doi: 10.1073/pnas.88.6.2515. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hauffe K. D., Paszkowski U., Schulze-Lefert P., Hahlbrock K., Dangl J. L., Douglas C. J. A parsley 4CL-1 promoter fragment specifies complex expression patterns in transgenic tobacco. Plant Cell. 1991 May;3(5):435–443. doi: 10.1105/tpc.3.5.435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hedrick S. A., Bell J. N., Boller T., Lamb C. J. Chitinase cDNA cloning and mRNA induction by fungal elicitor, wounding, and infection. Plant Physiol. 1988 Jan;86(1):182–186. doi: 10.1104/pp.86.1.182. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ichinose Y., Kawamata S., Yamada T., An C., Kajiwara T., Shiraishi T., Oku H. Molecular cloning of chalcone synthase cDNAs from Pisum sativum. Plant Mol Biol. 1992 Mar;18(5):1009–1012. doi: 10.1007/BF00019221. [DOI] [PubMed] [Google Scholar]
  10. Jacobsen K., Laursen N. B., Jensen E. O., Marcker A., Poulsen C., Marcker K. A. HMG I-like proteins from leaf and nodule nuclei interact with different AT motifs in soybean nodulin promoters. Plant Cell. 1990 Jan;2(1):85–94. doi: 10.1105/tpc.2.1.85. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jofuku K. D., Okamuro J. K., Goldberg R. B. Interaction of an embryo DNA binding protein with a soybean lectin gene upstream region. Nature. 1987 Aug 20;328(6132):734–737. doi: 10.1038/328734a0. [DOI] [PubMed] [Google Scholar]
  12. Joos H. J., Hahlbrock K. Phenylalanine ammonia-lyase in potato (Solanum tuberosum L.). Genomic complexity, structural comparison of two selected genes and modes of expression. Eur J Biochem. 1992 Mar 1;204(2):621–629. doi: 10.1111/j.1432-1033.1992.tb16675.x. [DOI] [PubMed] [Google Scholar]
  13. Katagiri F., Chua N. H. Plant transcription factors: present knowledge and future challenges. Trends Genet. 1992 Jan;8(1):22–27. doi: 10.1016/0168-9525(92)90020-5. [DOI] [PubMed] [Google Scholar]
  14. Kawamata S., Yamada T., Tanaka Y., Sriprasertsak P., Kato H., Ichinose Y., Kato H., Shiraishi T., Oku H. Molecular cloning of phenylalanine ammonia-lyase cDNA from Pisum sativum. Plant Mol Biol. 1992 Oct;20(1):167–170. doi: 10.1007/BF00029163. [DOI] [PubMed] [Google Scholar]
  15. Kiedrowski S., Kawalleck P., Hahlbrock K., Somssich I. E., Dangl J. L. Rapid activation of a novel plant defense gene is strictly dependent on the Arabidopsis RPM1 disease resistance locus. EMBO J. 1992 Dec;11(13):4677–4684. doi: 10.1002/j.1460-2075.1992.tb05572.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kuwabara M. D., Sigman D. S. Footprinting DNA-protein complexes in situ following gel retardation assays using 1,10-phenanthroline-copper ion: Escherichia coli RNA polymerase-lac promoter complexes. Biochemistry. 1987 Nov 17;26(23):7234–7238. doi: 10.1021/bi00397a006. [DOI] [PubMed] [Google Scholar]
  17. Lawton M. A., Lamb C. J. Transcriptional activation of plant defense genes by fungal elicitor, wounding, and infection. Mol Cell Biol. 1987 Jan;7(1):335–341. doi: 10.1128/mcb.7.1.335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lois R., Dietrich A., Hahlbrock K., Schulz W. A phenylalanine ammonia-lyase gene from parsley: structure, regulation and identification of elicitor and light responsive cis-acting elements. EMBO J. 1989 Jun;8(6):1641–1648. doi: 10.1002/j.1460-2075.1989.tb03554.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ohl S., Hedrick S. A., Chory J., Lamb C. J. Functional properties of a phenylalanine ammonia-lyase promoter from Arabidopsis. Plant Cell. 1990 Sep;2(9):837–848. doi: 10.1105/tpc.2.9.837. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pedersen T. J., Arwood L. J., Spiker S., Guiltinan M. J., Thompson W. F. High mobility group chromosomal proteins bind to AT-rich tracts flanking plant genes. Plant Mol Biol. 1991 Jan;16(1):95–104. doi: 10.1007/BF00017920. [DOI] [PubMed] [Google Scholar]
  21. Roth B. A., Goff S. A., Klein T. M., Fromm M. E. C1- and R-dependent expression of the maize Bz1 gene requires sequences with homology to mammalian myb and myc binding sites. Plant Cell. 1991 Mar;3(3):317–325. doi: 10.1105/tpc.3.3.317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sarokin L. P., Chua N. H. Binding sites for two novel phosphoproteins, 3AF5 and 3AF3, are required for rbcS-3A expression. Plant Cell. 1992 Apr;4(4):473–483. doi: 10.1105/tpc.4.4.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Schulze-Lefert P., Dangl J. L., Becker-André M., Hahlbrock K., Schulz W. Inducible in vivo DNA footprints define sequences necessary for UV light activation of the parsley chalcone synthase gene. EMBO J. 1989 Mar;8(3):651–656. doi: 10.1002/j.1460-2075.1989.tb03422.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Wingender R., Röhrig H., Höricke C., Wing D., Schell J. Differential regulation of soybean chalcone synthase genes in plant defence, symbiosis and upon environmental stimuli. Mol Gen Genet. 1989 Aug;218(2):315–322. doi: 10.1007/BF00331284. [DOI] [PubMed] [Google Scholar]
  25. da Costa e Silva O., Klein L., Schmelzer E., Trezzini G. F., Hahlbrock K. BPF-1, a pathogen-induced DNA-binding protein involved in the plant defense response. Plant J. 1993 Jul;4(1):125–135. doi: 10.1046/j.1365-313x.1993.04010125.x. [DOI] [PubMed] [Google Scholar]

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