Skip to main content
PMC home page
The Plant Cell logoLink to The Plant Cell
. 1993 Sep;5(9):1089–1099. doi: 10.1105/tpc.5.9.1089

Fungal Elicitor-Induced Bean Proline-Rich Protein mRNA Down-Regulation Is Due to Destabilization That Is Transcription and Translation Dependent.

S Zhang 1, J Sheng 1, Y Liu 1, MC Mehdy 1
PMCID: PMC160343  PMID: 12271097

Abstract

In bean cells treated with fungal elicitor, the transcripts of PvPRP1, a gene encoding a proline-rich protein, decreased to ~6% of the original level within 4 hr. The apparent mRNA half-life during the period of rapid degradation was ~45 min. The rate of PvPRP1 gene transcription remained constant over this period, as determined by nuclear run-off assays, indicating a decrease in mRNA stability. By using actinomycin D to block transcription, the half-life of PvPRP1 mRNA in unelicited cells was estimated to be ~60 hr. In cells treated with actinomycin D followed by the addition of elicitor, the PvPRP1 mRNA half-life was ~18 hr, whereas cells treated with these reagents in reciprocal order exhibited a half-life of ~6 hr. The protein synthesis inhibitors emetine and anisomycin also inhibited the rate of PvPRP1 mRNA degradation in elicited cells. Based on these data, we concluded that the rapid decrease in the PvPRP1 mRNA level in elicited cells is due to destabilization, which is dependent on new RNA and protein synthesis.

Full Text

The Full Text of this article is available as a PDF (2.8 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson-Prouty A. J., Albersheim P. Host-Pathogen Interactions: VIII. Isolation of a Pathogen-synthesized Fraction Rich in Glucan That Elicits a Defense Response in the Pathogen's Host. Plant Physiol. 1975 Aug;56(2):286–291. doi: 10.1104/pp.56.2.286. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bohjanen P. R., Petryniak B., June C. H., Thompson C. B., Lindsten T. An inducible cytoplasmic factor (AU-B) binds selectively to AUUUA multimers in the 3' untranslated region of lymphokine mRNA. Mol Cell Biol. 1991 Jun;11(6):3288–3295. doi: 10.1128/mcb.11.6.3288. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bradley D. J., Kjellbom P., Lamb C. J. Elicitor- and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: a novel, rapid defense response. Cell. 1992 Jul 10;70(1):21–30. doi: 10.1016/0092-8674(92)90530-p. [DOI] [PubMed] [Google Scholar]
  4. Brodl M. R., Ho T. H. Heat Shock Causes Selective Destabilization of Secretory Protein mRNAs in Barley Aleurone Cells. Plant Physiol. 1991 Aug;96(4):1048–1052. doi: 10.1104/pp.96.4.1048. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Casey J. L., Hentze M. W., Koeller D. M., Caughman S. W., Rouault T. A., Klausner R. D., Harford J. B. Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation. Science. 1988 May 13;240(4854):924–928. doi: 10.1126/science.2452485. [DOI] [PubMed] [Google Scholar]
  6. Cleveland D. W., Lopata M. A., Sherline P., Kirschner M. W. Unpolymerized tubulin modulates the level of tubulin mRNAs. Cell. 1981 Aug;25(2):537–546. doi: 10.1016/0092-8674(81)90072-6. [DOI] [PubMed] [Google Scholar]
  7. Dixon R. A., Harrison M. J. Activation, structure, and organization of genes involved in microbial defense in plants. Adv Genet. 1990;28:165–234. doi: 10.1016/s0065-2660(08)60527-1. [DOI] [PubMed] [Google Scholar]
  8. Edwards K., Cramer C. L., Bolwell G. P., Dixon R. A., Schuch W., Lamb C. J. Rapid transient induction of phenylalanine ammonia-lyase mRNA in elicitor-treated bean cells. Proc Natl Acad Sci U S A. 1985 Oct;82(20):6731–6735. doi: 10.1073/pnas.82.20.6731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gay D. A., Sisodia S. S., Cleveland D. W. Autoregulatory control of beta-tubulin mRNA stability is linked to translation elongation. Proc Natl Acad Sci U S A. 1989 Aug;86(15):5763–5767. doi: 10.1073/pnas.86.15.5763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Guerrero F., Mullet J. E. Increased Abscisic Acid Biosynthesis during Plant Dehydration Requires Transcription. Plant Physiol. 1986 Feb;80(2):588–591. doi: 10.1104/pp.80.2.588. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Han I. S., Jongewaard I., Fosket D. E. Limited expression of a diverged beta-tubulin gene during soybean (Glycine max [L.] Merr.) development. Plant Mol Biol. 1991 Feb;16(2):225–234. doi: 10.1007/BF00020554. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Hofer E., Hofer-Warbinek R., Darnell J. E., Jr Globin RNA transcription: a possible termination site and demonstration of transcriptional control correlated with altered chromatin structure. Cell. 1982 Jul;29(3):887–893. doi: 10.1016/0092-8674(82)90450-0. [DOI] [PubMed] [Google Scholar]
  14. Jones T. R., Cole M. D. Rapid cytoplasmic turnover of c-myc mRNA: requirement of the 3' untranslated sequences. Mol Cell Biol. 1987 Dec;7(12):4513–4521. doi: 10.1128/mcb.7.12.4513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kruijer W., Cooper J. A., Hunter T., Verma I. M. Platelet-derived growth factor induces rapid but transient expression of the c-fos gene and protein. Nature. 1984 Dec 20;312(5996):711–716. doi: 10.1038/312711a0. [DOI] [PubMed] [Google Scholar]
  16. Laird-Offringa I. A. What determines the instability of c-myc proto-oncogene mRNA? Bioessays. 1992 Feb;14(2):119–124. doi: 10.1002/bies.950140209. [DOI] [PubMed] [Google Scholar]
  17. Lam E., Green P. J., Wong M., Chua N. H. Phytochrome activation of two nuclear genes requires cytoplasmic protein synthesis. EMBO J. 1989 Oct;8(10):2777–2783. doi: 10.1002/j.1460-2075.1989.tb08423.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. 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]
  19. Müller R., Bravo R., Burckhardt J., Curran T. Induction of c-fos gene and protein by growth factors precedes activation of c-myc. Nature. 1984 Dec 20;312(5996):716–720. doi: 10.1038/312716a0. [DOI] [PubMed] [Google Scholar]
  20. Müllner E. W., Kühn L. C. A stem-loop in the 3' untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm. Cell. 1988 Jun 3;53(5):815–825. doi: 10.1016/0092-8674(88)90098-0. [DOI] [PubMed] [Google Scholar]
  21. Nagase T., Mizuguchi G., Nomura N., Ishizaki R., Ueno Y., Ishii S. Requirement of protein co-factor for the DNA-binding function of the human ski proto-oncogene product. Nucleic Acids Res. 1990 Jan 25;18(2):337–343. doi: 10.1093/nar/18.2.337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pachter J. S., Yen T. J., Cleveland D. W. Autoregulation of tubulin expression is achieved through specific degradation of polysomal tubulin mRNAs. Cell. 1987 Oct 23;51(2):283–292. doi: 10.1016/0092-8674(87)90155-3. [DOI] [PubMed] [Google Scholar]
  23. Ross J., Pizarro A. Human beta and delta globin messenger RNAs turn over at different rates. J Mol Biol. 1983 Jul 5;167(3):607–617. doi: 10.1016/s0022-2836(83)80101-6. [DOI] [PubMed] [Google Scholar]
  24. Ryder T. B., Cramer C. L., Bell J. N., Robbins M. P., Dixon R. A., Lamb C. J. Elicitor rapidly induces chalcone synthase mRNA in Phaseolus vulgaris cells at the onset of the phytoalexin defense response. Proc Natl Acad Sci U S A. 1984 Sep;81(18):5724–5728. doi: 10.1073/pnas.81.18.5724. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Shyu A. B., Greenberg M. E., Belasco J. G. The c-fos transcript is targeted for rapid decay by two distinct mRNA degradation pathways. Genes Dev. 1989 Jan;3(1):60–72. doi: 10.1101/gad.3.1.60. [DOI] [PubMed] [Google Scholar]
  26. Silflow C. D., Key J. L. Stability of polysome-associated polyadenylated RNA from soybean suspension culture cells. Biochemistry. 1979 Mar 20;18(6):1013–1018. doi: 10.1021/bi00573a013. [DOI] [PubMed] [Google Scholar]
  27. Thompson D. M., Meagher R. B. Transcriptional and post-transcriptional processes regulate expression of RNA encoding the small subunit of ribulose-1,5-biphosphate carboxylase differently in petunia and in soybean. Nucleic Acids Res. 1990 Jun 25;18(12):3621–3629. doi: 10.1093/nar/18.12.3621. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Thompson D. M., Tanzer M. M., Meagher R. B. Degradation products of the mRNA encoding the small subunit of ribulose-1,5-bisphosphate carboxylase in soybean and transgenic petunia. Plant Cell. 1992 Jan;4(1):47–58. doi: 10.1105/tpc.4.1.47. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Walling L., Drews G. N., Goldberg R. B. Transcriptional and post-transcriptional regulation of soybean seed protein mRNA levels. Proc Natl Acad Sci U S A. 1986 Apr;83(7):2123–2127. doi: 10.1073/pnas.83.7.2123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Wilson T., Treisman R. Removal of poly(A) and consequent degradation of c-fos mRNA facilitated by 3' AU-rich sequences. Nature. 1988 Nov 24;336(6197):396–399. doi: 10.1038/336396a0. [DOI] [PubMed] [Google Scholar]
  31. Wisdom R., Lee W. The protein-coding region of c-myc mRNA contains a sequence that specifies rapid mRNA turnover and induction by protein synthesis inhibitors. Genes Dev. 1991 Feb;5(2):232–243. doi: 10.1101/gad.5.2.232. [DOI] [PubMed] [Google Scholar]

Articles from The Plant Cell are provided here courtesy of Oxford University Press

RESOURCES