title: Ray38p, a homolog of a purine motif triple-helical DNA-binding protein, Stm1p, is a ribosome-associated protein and dissociated from ribosomes prior to the induction of cycloheximide resistance in Candida maltosa.
abstract: Cycloheximide (CYH) resistance in Candida maltosa is dependent on the induction of a ribosomal protein, Q-type L41, the 56th residue of which is glutamine, not proline as in ordinary P-type L41. We found that a 38-kDa protein in a wild-type C. maltosa ribosomal fraction became undetectable upon CYH treatment but detectable again with the establishment of CYH resistance by the induction of Q-type L41. We cloned a gene coding for this protein and named it RAY38 (ribosome-associated protein of yeast). Ray38p is a homolog of a purine motif triple-helical DNA-binding protein, Stm1p, and has a putative RNA-binding motif RGG. The ribosome-associated Ray38p was phosphorylated at serine and threonine residues, and Ray38p that was dissociated from ribosome by CYH treatment was highly phosphorylated in threonine residues. A ray38 null mutant recovered faster from CYH-caused growth stasis than the wild-type strain, suggesting that the dissociation of Ray38p from ribosome facilitates the induction of CYH resistance in C. maltosa.
authors.affiliation: Department of Biotechnology, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Takaku
authors.forename: E
authors.initials: E
authors.lastname: Mutoh
authors.forename: H
authors.initials: H
authors.lastname: Horiuchi
authors.forename: A
authors.initials: A
authors.lastname: Ohta
authors.forename: M
authors.initials: M
authors.lastname: Takagi
mesh_terms: D020816:Amino Acid Motifs / Q000235:genetics; D019943:Amino Acid Substitution; D001483:Base Sequence; D002175:Candida / Q000187:drug effects* / Q000378:metabolism; D002455:Cell Division / Q000187:drug effects / Q000235:genetics; D003513:Cycloheximide / Q000494:pharmacology*; D039642:Eukaryotic Initiation Factors; D005656:Fungal Proteins / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009154:Mutation; D010448:Peptide Initiation Factors; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D012316:RNA Nucleotidyltransferases / Q000235:genetics*; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000378:metabolism; D013347:Subcellular Fractions / Q000737:chemistry; D013696:Temperature; D013912:Threonine / Q000378:metabolism
chemical_list: D039642:Eukaryotic Initiation Factors; D005656:Fungal Proteins; D010448:Peptide Initiation Factors; D010750:Phosphoproteins; D011500:Protein Synthesis Inhibitors; C430504:Ray38 protein, Candida maltosa; D012269:Ribosomal Proteins; D029701:Saccharomyces cerevisiae Proteins; C083432:TIF3 protein, S cerevisiae; D013912:Threonine; D012694:Serine; D003513:Cycloheximide; D012316:RNA Nucleotidyltransferases