1887

Abstract

Survival of micro-organisms in natural habitats depends on their ability to adapt to variations in osmotic conditions. We previously described the gene of , encoding a protein of the haloacid dehalogenase family with an unknown function in the osmotic stress response. Here we report on the functional analysis of , the orthologous gene in the phytopathogenic fungus . mRNA levels increased transiently after exposure to 0.68 M NaCl and were reduced upon return to normal osmotic conditions; deletion of the gene resulted in a partial reduction in tolerance to osmotic stress. Δ mutants contained much lower intracellular levels of glycerol than the wild-type, and did not exhibit the increase following hyper-osmotic shock expected from the high osmolarity glycerol (HOG) response. is linked and divergently transcribed with the putative glycerol dehydrogenase gene , which showed the same regulation by osmotic shock. The intergenic / regulatory region contains putative stress-response elements conserved in other fungi, and both genes shared other regulatory features, such as induction by heat shock and by illumination. Photoinduction was also observed in the HOG response gene , and was lost in mutants of the white collar gene . Previous data on glycerol production in spp. and features of the predicted CutA protein lead us to propose that produces glycerol from dihydroxyacetone, and that CutA is the enzyme involved in the synthesis of this precursor by dephosphorylation of dihydroxyacetone-3P.

Funding
This study was supported by the:
  • Spanish Government (Ministerio de Ciencia y Tecnología (Award BIO2009-11131 and BIO2006-01323)
  • Andalusian Government (Award CTS-6638 and P07-CVI-02813)
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2014-01-01
2024-04-20
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