Abstract

In this study, the roles of fungal dehydrin-like proteins in pathogenicity and protection against environmental stresses were investigated in the necrotrophic seed-borne fungus Alternaria brassicicola. Three proteins (called AbDhn1, AbDhn2 and AbDhn3), harbouring the asparagine-proline-arginine (DPR) signature pattern and sharing the characteristic features of fungal dehydrin-like proteins, were identified in the A. brassicicola genome. The expression of these genes was induced in response to various stresses and found to be regulated by the AbHog1 mitogen-activated protein kinase (MAPK) pathway. A knock-out approach showed that dehydrin-like proteins have an impact mainly on oxidative stress tolerance and on conidial survival upon exposure to high and freezing temperatures. The subcellular localization revealed that AbDhn1 and AbDhn2 were associated with peroxisomes, which is consistent with a possible perturbation of protective mechanisms to counteract oxidative stress and maintain the redox balance in AbDhn mutants. Finally, we show that the double deletion mutant ΔΔabdhn1-abdhn2 was highly compromised in its pathogenicity. By comparison to the wild-type, this mutant exhibited lower aggressiveness on B. oleracea leaves and a reduced capacity to be transmitted to Arabidopsis seeds via siliques. The double mutant was also affected with respect to conidiation, another crucial step in the epidemiology of the disease.

Highlights

  • Dehydrins belong to the 2a and 2b groups of the large late embryogenesis-abundant (LEA) protein family [1,2], which were initially described as accumulating late in plant seed development

  • Three proteins harbouring the fungal dehydrin signature pattern were identified from the A. brassicicola genome

  • In silico analyses confirmed that they shared the characteristic features of dehydrin-like proteins via their physicochemical properties

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Summary

Introduction

Dehydrins belong to the 2a and 2b groups of the large late embryogenesis-abundant (LEA) protein family [1,2], which were initially described as accumulating late in plant seed development. They were found in vegetative plant tissues following environmental stresses and are believed to play a role in the protection against cold- and dehydration-related stresses [3,4,5]. Their amino acid composition is characterized by high percentages of glycine, threonine and serine, and low levels of cysteine and tryptophan residues.

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