Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1997 Nov;115(3):1021–1027. doi: 10.1104/pp.115.3.1021

Histone Hyperacetylation in Maize in Response to Treatment with HC-Toxin or Infection by the Filamentous Fungus Cochliobolus carbonum.

R F Ransom 1, J D Walton 1
PMCID: PMC158565  PMID: 12223856

Abstract

HC-toxin, the host-selective toxin produced by the filamentous fungus Cochliobolus carbonum, inhibits maize (Zea mays L.) histone deacetylases (HDs) in vitro. Here we show that HDs are also inhibited by HC-toxin in vivo, as demonstrated by the accumulation of hyperacetylated forms of the core (nucleosomal) histones H3.1, H3.2, H3.3, and H4 in both maize embryos and tissue cultures. Hyperacetylation of H4 and all isoforms of H3 in tissue cultures of inbred Pr (genotype hm/hm) occurred at 10 ng/mL (23 nM). The effect was host-selective; acetylation of histones in the near isogenic inbred Pr1 (genotype Hm/Hm) did not occur in tissue cultures or embryos treated with 0.2 [mu]g/mL or 10 [mu]g/mL HC-toxin, respectively. Hyperacetylation of histone H4 in embryos of Pr1 began to occur at 50 [mu]g/mL. HC-toxin, and 200 [mu]g/mL HC-toxin caused equal hyperacetylation in Pr and Pr1 embryos. Hyperacetylated core histones, especially of the isoforms of histone H3, accumulated in leaves of inbred Pr, but not Pr1, after infection by toxin-producing strains of C. carbonum. Accumulation of hyperacetylated histones began at 24 h after inoculation, before the development of visible disease symptoms. Hyperacetylation of H2A or H2B histones were not detected in any of the studies. The results are consistent with HD being a primary site of action of HC-toxin.

Full Text

The Full Text of this article is available as a PDF (2.2 MB).

Selected References

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

  1. Brosch G., Ransom R., Lechner T., Walton J. D., Loidl P. Inhibition of maize histone deacetylases by HC toxin, the host-selective toxin of Cochliobolus carbonum. Plant Cell. 1995 Nov;7(11):1941–1950. doi: 10.1105/tpc.7.11.1941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Darkin-Rattray S. J., Gurnett A. M., Myers R. W., Dulski P. M., Crumley T. M., Allocco J. J., Cannova C., Meinke P. T., Colletti S. L., Bednarek M. A. Apicidin: a novel antiprotozoal agent that inhibits parasite histone deacetylase. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):13143–13147. doi: 10.1073/pnas.93.23.13143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Johal G. S., Briggs S. P. Reductase activity encoded by the HM1 disease resistance gene in maize. Science. 1992 Nov 6;258(5084):985–987. doi: 10.1126/science.1359642. [DOI] [PubMed] [Google Scholar]
  4. Lusser A., Brosch G., Loidl A., Haas H., Loidl P. Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein. Science. 1997 Jul 4;277(5322):88–91. doi: 10.1126/science.277.5322.88. [DOI] [PubMed] [Google Scholar]
  5. Meeley R. B., Walton J. D. Enzymatic Detoxification of HC-toxin, the Host-Selective Cyclic Peptide from Cochliobolus carbonum. Plant Physiol. 1991 Nov;97(3):1080–1086. doi: 10.1104/pp.97.3.1080. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Rundlett S. E., Carmen A. A., Kobayashi R., Bavykin S., Turner B. M., Grunstein M. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14503–14508. doi: 10.1073/pnas.93.25.14503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Van Lint C., Emiliani S., Verdin E. The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr. 1996;5(4-5):245–253. [PMC free article] [PubMed] [Google Scholar]
  8. Walton J. D., Earle E. D., Gibson B. W. Purification and structure of the host-specific toxin from Helminthosporium carbonum race 1. Biochem Biophys Res Commun. 1982 Aug;107(3):785–794. doi: 10.1016/0006-291x(82)90592-7. [DOI] [PubMed] [Google Scholar]
  9. Walton J. D., Earle E. D., Stähelin H., Grieder A., Hirota A., Suzuki A. Reciprocal biological activities of the cyclic tetrapeptides chlamydocin and HC-toxin. Experientia. 1985 Mar 15;41(3):348–350. doi: 10.1007/BF02004498. [DOI] [PubMed] [Google Scholar]
  10. Walton J. D. Host-selective toxins: agents of compatibility. Plant Cell. 1996 Oct;8(10):1723–1733. doi: 10.1105/tpc.8.10.1723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Waterborg J. H., Harrington R. E., Winicov I. Differential Histone Acetylation in Alfalfa (Medicago sativa) Due to Growth in NaCl : Responses in Salt Stressed and Salt Tolerant Callus Cultures. Plant Physiol. 1989 May;90(1):237–245. doi: 10.1104/pp.90.1.237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Waterborg J. H., Harrington R. E., Winicov I. Dynamic histone acetylation in alfalfa cells. Butyrate interference with acetate labeling. Biochim Biophys Acta. 1990 Jul 30;1049(3):324–330. doi: 10.1016/0167-4781(90)90105-b. [DOI] [PubMed] [Google Scholar]
  13. Waterborg J. H. Multiplicity of histone h3 variants in wheat, barley, rice, and maize. Plant Physiol. 1991 Jun;96(2):453–458. doi: 10.1104/pp.96.2.453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Waterborg J. H., Winicov I., Harrington R. E. Histone variants and acetylated species from the alfalfa plant Medicago sativa. Arch Biochem Biophys. 1987 Jul;256(1):167–178. doi: 10.1016/0003-9861(87)90435-8. [DOI] [PubMed] [Google Scholar]
  15. Yoder O. C., Scheffer R. P. Effects of Helminthosporium carbonum Toxin on Nitrate Uptake and Reduction by Corn Tissues. Plant Physiol. 1973 Dec;52(6):513–517. doi: 10.1104/pp.52.6.513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Yoshida M., Kijima M., Akita M., Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem. 1990 Oct 5;265(28):17174–17179. [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES