Summary: The salt-tolerant yeast can adjust its osmotic balance when responding to osmotic shock by accumulating glycerol as the compatible osmolyte. However, the mechanism of glycerol production in cells and its genetic regulation remain to be elucidated. Two putative mitogen-activated protein (MAP) kinase genes, and were cloned from by their homology with from The deduced amino acid sequences of ZrHog1p and ZrHog2p indicated close homology to that of Hog1p and contained a TGY motif for phosphorylation by MAP kinase kinase. When or was expressed in an null mutant, the salt tolerance and osmotic tolerance characteristics of wild-type were restored. In addition, the aberrant cell morphology and low glycerol content of the Δ null mutant were corrected, indicating that ZrHog1p and ZrHog2p have functions similar to Hog1p. While the transcription of the glycerol-3-phosphate dehydrogenase gene () of the -harbouring mutant was similar to that of wild-type the -harbouring strain showed prolonged transcription. Both Δ and Δ null mutants showed a decrease in salt tolerance compared to the wild-type strain. The present study suggested the presence of a high-osmolarity glycerol response (HOG) pathway in similar to that elucidated in Two putative MAP kinase genes in appeared to be significant in either osmotic regulation or ion homeostasis.


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