KlHsl1 is a component of glycerol response pathways in the milk yeast Kluyveromyces lactis
Author(s) -
Samantha Cialfi,
Daniela Uccelletti,
A. Carducci,
Micheline WésolowskiLouvel,
Patrizia Mancini,
Hermann J. Heipieper,
Michele Saliola
Publication year - 2011
Publication title -
microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 179
eISSN - 1465-2080
pISSN - 1350-0872
DOI - 10.1099/mic.0.044040-0
Subject(s) - kluyveromyces lactis , biology , kluyveromyces , saccharomyces cerevisiae , mutant , biochemistry , threonine , yeast , microbiology and biotechnology , antimycin a , protein kinase a , kinase , serine , phosphorylation , gene , mitochondrion
In Saccharomyces cerevisiae, HSL1 (NIK1) encodes a serine-threonine protein kinase involved in cell cycle control and morphogenesis. Deletion of its putative orthologue in Kluyveromyces lactis, KlHSL1, gives rise to sensitivity to the respiratory inhibitor antimycin A (AA). Resistance to AA on glucose (Rag+ phenotype) is associated with genes (RAG) required for glucose metabolism/glycolysis. To understand the relationship between RAG and KlHSL1, rag and Klhsl1Δ mutant strains were investigated. The analysis showed that all the mutants contained a phosphorylated form of Hog1 and displayed an inability to synthesize/accumulate glycerol as a compatible solute. In addition, rag mutants also showed alterations in both cell wall and membrane fatty acids. The pleiotropic defects of these strains indicate that a common pathway regulates glucose utilization and stress response mechanisms, suggesting impaired adaptation of the plasma membrane/cell wall during the respiratory-fermentative transition. KlHsl1 could be the link between these adaptive pathways and the morphogenetic checkpoint.
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