期刊
MICROBIOLOGY-SGM
卷 153, 期 -, 页码 4016-4026出版社
MICROBIOLOGY SOC
DOI: 10.1099/mic.0.2007/010298-0
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- Biotechnology and Biological Sciences Research Council [BB/C007077/1, BB/C000072/1] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [BB/C000072/1, BB/C007077/1] Funding Source: researchfish
In Saccharomyces cerevisiae, the serine-threonine protein kinase activity of Dbf2p is required for tolerance to the weak organic acid sorbic acid. Here we show that Dbf2p is required for normal phosphorylation of the vacuolar H+-ATPase (V-ATPase) A and B subunits Vma1p and Vma2p. Loss of V-ATPase activity due to bafilomycin treatment or deletion of either VMA1 or VMA2 resulted in sorbic acid hypersensitivity and impaired vacuolar acidification, phenotypes also observed in both a kinase-inactive dbf2 mutant and cells completely lacking DBF2 (dbf2 Delta). Crucially, VMA2 is a multicopy suppressor of both the sorbic acid-sensitive phenotype and the impaired vacuolar-acidification defect of dbf2 Delta cells, confirming a functional interaction between Dbf2p and Vma2p. The yeast V-ATPase is therefore involved in mediating sorbic acid stress tolerance, and we have shown a novel and unexpected role for the cell cycle-regulated protein kinase Dbf2p in promoting V-ATPase function.
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