title: A serine/threonine protein phosphatase-like protein, CaPTC8, from Candida albicans defines a new PPM subfamily.
abstract: Protein phosphatase M family (PPM; Mg(2+)-dependent protein phosphatases), which specifically dephosphorylates serine/threonine residues, consists of pyruvate dehydrogenase phosphatases, SpoIIE, adenylate cyclase and protein phosphatase type 2Cs (PP2Cs). To identify Candida albicans PP2Cs, the archetype of the PPM Ser/Thr phosphatases, we thoroughly searched the public C. albicans genome database and identified seven PP2C members. One of the PP2Cs in C. albicans, designated as CaPTC8 gene, represents a new member of PP2C genes. Northern blot analysis showed that the expression of CaPTC8 was positively responsive to high osmolarity, temperature or serum-stimulated filamentous growth. Gene disruption further demonstrated that deletion of CaPTC8 gene caused the defect of hyphal formation. Sequence analysis revealed that two conserved amino acids His and Asn in the prototypical members of the PPM family were substituted by Val and Asp in the PTC8p-like proteins. In addition, posterior analysis for site-specific profile showed that seven more sites are under the selection of functional divergence between these two groups of proteins. Three-dimensional homology modeling illustrated the signatures of the two groups in the conserved catalytic region of the protein phosphatases. Hence, CaPTC8 plays a role in stress responses and is required for the yeast-hyphal transition, and the CaPTC8-related genes are evolutionarily conserved. The phylogenetic relationships of all members of the PPM family strongly support the existence of a distinct and new subfamily of the PP2C-related proteins, PP2CR.
authors.affiliation: Mammalian Cell Genetics Group, Health Sector, Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec, Canada H4P 2R2. jinjiang.fan@mail.mcgill.ca
authors.forename: Jinjiang
authors.initials: J
authors.lastname: Fan
authors.forename: Meiqun
authors.initials: M
authors.lastname: Wu
authors.forename: Linghuo
authors.initials: L
authors.lastname: Jiang
authors.forename: Shi-Hsiang
authors.initials: SH
authors.lastname: Shen
mesh_terms: D000262:Adenylyl Cyclases / Q000737:chemistry; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D055162:Biocatalysis; D002176:Candida albicans / Q000166:cytology / Q000201:enzymology* / Q000235:genetics; D017124:Conserved Sequence; D019143:Evolution, Molecular; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D005800:Genes, Fungal; D006801:Humans; D025301:Hyphae / Q000166:cytology / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D010641:Phenotype; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D000071636:Protein Phosphatase 2C; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013312:Stress, Physiological; D040681:Structural Homology, Protein
chemical_list: D005656:Fungal Proteins; D010749:Phosphoprotein Phosphatases; D000071636:Protein Phosphatase 2C; D000262:Adenylyl Cyclases