HISTONE DEACETYLASE 6 represses pathogen defence responses in Arabidopsis thaliana

Plant Cell Environ. 2017 Dec;40(12):2972-2986. doi: 10.1111/pce.13047. Epub 2017 Oct 30.

Abstract

Plant defence mechanisms are suppressed in the absence of pathogen attack to prevent wasted energy and growth inhibition. However, how defence responses are repressed is not well understood. Histone deacetylase 6 (HDA6) is a negative regulator of gene expression, and its role in pathogen defence response in plants is not known. In this study, a novel allele of hda6 (designated as shi5) with spontaneous defence response was isolated from a forward genetics screening in Arabidopsis. The shi5 mutant exhibited increased resistance to hemibiotrophic bacterial pathogen Pst DC3000, constitutively activated expression of pathogen-responsive genes including PR1, PR2, etc. and increased histone acetylation levels at the promoters of most tested genes that were upregulated in shi5. In both wild type and shi5 plants, the expression and histone acetylation of these genes were upregulated by pathogen infection. HDA6 was found to bind to the promoters of these genes under both normal growth conditions and pathogen infection. Our research suggests that HDA6 is a general repressor of pathogen defence response and plays important roles in inhibiting and modulating the expression of pathogen-responsive genes in Arabidopsis.

Keywords: HDA6; basal immunity; gene repression.

MeSH terms

  • Acetylation
  • Alleles
  • Arabidopsis / enzymology*
  • Arabidopsis / genetics
  • Arabidopsis / immunology
  • Arabidopsis / microbiology
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Gene Expression Regulation, Plant
  • Histone Deacetylases / genetics
  • Histone Deacetylases / metabolism*
  • Host-Pathogen Interactions*
  • Mutation
  • Plant Diseases / immunology*
  • Plant Diseases / microbiology
  • Plant Immunity*
  • Pseudomonas / physiology*

Substances

  • Arabidopsis Proteins
  • HDA6 protein, Arabidopsis
  • Histone Deacetylases