title: Subcellular localization of the histidine kinase receptors Sln1p, Nik1p and Chk1p in the yeast CTG clade species Candida guilliermondii.
abstract: Fungal histidine kinase receptors (HKR) sense and transduce many intra- and extracellular signals that regulate a wide range of physiological processes. Candida CTG clade species commonly possess three types of HKR namely Sln1p (type VI), Nik1p (type III) and Chk1p (type X). Although some recent work has demonstrated the potential involvement of HKR in osmoregulation, morphogenesis, sexual development, adaptation to osmotic stresses and drug resistance in distinct Candida species, little data is available in relation to their subcellular distribution within yeast cells. We describe in this work the comparative subcellular localization of class III, VI, and X HKRs in Candida guilliermondii, a yeast CTG clade species of clinical and biotechnological interest. Using a fluorescent protein fusion approach, we showed that C. guilliermondii Sln1p fused to the yellow fluorescent protein (Sln1p-YFP) appeared to be anchored in the plasma membrane. By contrast, both Chk1p-YFP and YFP-Chk1p were localized in the nucleocytosol of C. guilliermondii transformed cells. Furthermore, while Nik1p-YFP fusion protein always displayed a nucleocytosolic localization, we noted that most of the cells expressing YFP-Nik1p fusion protein displayed an aggregated pattern of fluorescence in the cytosol but not in the nucleus. Interestingly, Sln1p-YFP and Nik1p-YFP fusion protein localization changed in response to hyperosmotic stress by rapidly clustering into punctuated structures that could be associated to osmotic stress signaling. To date, this work provides the first insight into the subcellular localization of the three classes of HKR encoded by CTG clade yeast genomes and constitutes original new data concerning this family of receptors. This represents also an essential prerequisite to open a window into the understanding of the global architecture of HKR-mediated signaling pathways in CTG clade species.
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
authors: Emilien
authors: E
authors: Foureau
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
authors: Marc
authors: M
authors: Clastre
authors: Universidad de Antioquia, Laboratorio de Biotecnología, Sede de Investigación Universitaria, Colombia.
authors: Erika J Obando
authors: EJ
authors: Montoya
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
authors: Sébastien
authors: S
authors: Besseau
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
authors: Audrey
authors: A
authors: Oudin
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
authors: Gaëlle
authors: G
authors: Glévarec
authors: University of Essex, Department of Biological Sciences, Wivenhoe Park, Colchester, United Kingdom.
authors: Andrew J
authors: AJ
authors: Simkin
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
authors: Joël
authors: J
authors: Crèche
authors: Universidad de Antioquia, Laboratorio de Biotecnología, Sede de Investigación Universitaria, Colombia.
authors: Lucia
authors: L
authors: Atehortùa
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
authors: Nathalie
authors: N
authors: Giglioli-Guivarc'h
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
authors: Vincent
authors: V
authors: Courdavault
authors: Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France. Electronic address: nicolas.papon@univ-tours.fr.
authors: Nicolas
authors: N
authors: Papon
mesh_terms: D002175:Candida / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D000071677:Histidine Kinase; D009997:Osmotic Pressure; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D005656:Fungal Proteins; D011494:Protein Kinases; D000071677:Histidine Kinase
keywords: Candida guilliermondii; Cell signaling; Fluorescent protein; Histidine kinase receptors; Multistep phosphorelay