title: Phosphorylation of mitochondrial telomere binding protein of Candida parapsilosis by camp-dependent protein kinase.
abstract: Mitochondrial telomere-binding protein (mtTBP) of Candida parapsilosis binds with high affinity to 5' single-stranded overhang of the linear mitochondrial DNA of this yeast (Tomáska, L'., Nosek, J., and Fukuhara, H. (1997) J. Biol. Chem. 272, 3049-3056). Here it is reported that mtTBP is phosphorylated by catalytic subunit of cAMP-dependent protein kinase in vitro. Phosphorylated mtTBP has dramatically reduced ability to bind telomeric oligonucleotide in the gel-mobility retardation assay without affecting the oligomerization of mtTBP in vitro. MtTBP is one of the few mitochondrial proteins and the first mitochondrial single-strand DNA binding proteins that was demonstrated to serve as a substrate for cAMP-dependent protein kinase.
authors.affiliation: Department of Genetics, Faculty of Natural Sciences, Comenius University, Bratislava, Slovakia.
authors.forename: L
authors.initials: L
authors.lastname: Tomáska
mesh_terms: D002175:Candida / Q000378:metabolism*; D003432:Cross-Linking Reagents / Q000378:metabolism; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D004272:DNA, Mitochondrial / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000032:analysis / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D005976:Glutaral / Q000378:metabolism; D008928:Mitochondria / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D016615:Telomere / Q000378:metabolism*
chemical_list: D003432:Cross-Linking Reagents; D004272:DNA, Mitochondrial; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D017868:Cyclic AMP-Dependent Protein Kinases; D005976:Glutaral