title: KlHsl1 is a component of glycerol response pathways in the milk yeast Kluyveromyces lactis.
abstract: 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.
authors.affiliation: Department of Biology and Biotechnology 'C. Darwin', University of Rome 'La Sapienza', Piazzale Aldo Moro 5, 00185 Rome, Italy.
authors.forename: Samantha
authors.initials: S
authors.lastname: Cialfi
authors.affiliation: Department of Biology and Biotechnology 'C. Darwin', University of Rome 'La Sapienza', Piazzale Aldo Moro 5, 00185 Rome, Italy.
authors.forename: Daniela
authors.initials: D
authors.lastname: Uccelletti
authors.affiliation: Department of Biology and Biotechnology 'C. Darwin', University of Rome 'La Sapienza', Piazzale Aldo Moro 5, 00185 Rome, Italy.
authors.forename: Augusto
authors.initials: A
authors.lastname: Carducci
authors.affiliation: UMR, Microbiologie, Adaptation et Pathogénie, Université de Lyon, Lyon, F-69003, France; Université Lyon 1, Lyon, F-69003, France; CNRS, Villeurbanne, F-69622, France; and INSA de Lyon, Villeurbanne, F-69621, France.
authors.forename: Micheline
authors.initials: M
authors.lastname: Wésolowski-Louvel
authors.affiliation: Department of Experimental Medicine, University of Rome 'La Sapienza', Viale Regina Elena 324, 00161 Rome, Italy.
authors.forename: Patrizia
authors.initials: P
authors.lastname: Mancini
authors.affiliation: Department of Environmental Biotechnology, Helmholtz Centre for Environmental Research - UFZ, Permoserstrasse 15, 04318 Leipzig, Germany.
authors.forename: Hermann J
authors.initials: HJ
authors.lastname: Heipieper
authors.affiliation: Department of Biology and Biotechnology 'C. Darwin', University of Rome 'La Sapienza', Piazzale Aldo Moro 5, 00185 Rome, Italy.
authors.forename: Michele
authors.initials: M
authors.lastname: Saliola
mesh_terms: D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal; D005990:Glycerol / Q000378:metabolism*; D007716:Kluyveromyces / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion
chemical_list: D005656:Fungal Proteins; D017346:Protein Serine-Threonine Kinases; D005990:Glycerol