title: Nuclear thioredoxin peroxidase Dot5 in Saccharomyces cerevisiae: roles in oxidative stress response and disruption of telomeric silencing.
abstract: The DOT5 gene was originally cloned as one of the DOT (disrupter of telomeric silencing) genes; and later it was re-discovered as a nuclear thioredoxin peroxidase in Saccharomyces cerevisiae. Here, we demonstrate that the telomeric-silencing disruption activity of Dot5 is independent of thioredoxin peroxidase activity. In addition, Dot5 cannot suppress the increased susceptibility to peroxides of mutants defected in cytosolic thioredoxin peroxidase, even when Dot5 is expressed in the cytoplasm. Furthermore, Dot5 does not affect redox regulation of the Yap1 transcription factor. These results suggest that Dot5 is less important as an antioxidant in yeast cells.
authors.affiliation: Laboratory of Molecular Microbiology, Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Uji, 611-0011 Kyoto, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Izawa
authors.forename: N
authors.initials: N
authors.lastname: Kuroki
authors.forename: Y
authors.initials: Y
authors.lastname: Inoue
mesh_terms: D002467:Cell Nucleus / Q000201:enzymology; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000201:enzymology; D017353:Gene Deletion; D015966:Gene Expression Regulation, Fungal; D005800:Genes, Fungal; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D054464:Peroxiredoxins; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D016615:Telomere / Q000502:physiology*; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; C086677:YAP1 protein, S cerevisiae; D010544:Peroxidases; D054464:Peroxiredoxins