title: Respiration, copper availability and SOD activity in P. anserina strains with different lifespan.
abstract: P. anserina mutants with impairments in complex IV (COX) of the respiratory chain are characterized by an increase in lifespan. Examples are the nuclear grisea mutant with a moderate lifespan extension (60%) and the immortal extranuclear ex1 mutant. Here we report data demonstrating that in mutant ex1 the level of the alternative oxidase (PaAOX) is significantly higher than in mutant grisea. PaAOX levels appear to be reversely dependent on COX activity. The activity profile of superoxide dismutases in the ex1 mutant resembles the profile in senescent wild-type cultures with a high cytoplasmic copper/zinc superoxide dismutase (PaSOD1) and a low mitochondrial manganese superoxide dismutase (PaSOD2) activity. In the grisea mutant, PaSOD1 activity is only detectable in cultures grown in copper-supplemented medium. The two copper-regulated genes PaCtr3 (coding for a high affinity copper transporter) and PaSod2 are not expressed in the two mutants grown in standard medium. The repression of these genes as well as the activity of PaSOD1 is dependent on the availability of cellular copper, which appears to be high in COX-deficient strains such as mutant ex1 and in the senescent wild-type strain. In the wild-type, changes in the cellular localization of copper and in the delivery of this metal to different proteins appear to occur during senescence. Collectively, the data explain the characteristic lifespan of the investigated strains as the result of differences in energy transduction and in the machinery protecting against oxidative stress.
authors.affiliation: Johann Wolfgang Goethe-Universität, Botanisches Institut, Marie-Curie-Strasse 9, 60439 Frankfurt am Main, Germany.
authors.forename: Corina
authors.initials: C
authors.lastname: Borghouts
authors.forename: Christian Q
authors.initials: CQ
authors.lastname: Scheckhuber
authors.forename: Alexandra
authors.initials: A
authors.lastname: Werner
authors.forename: Heinz D
authors.initials: HD
authors.lastname: Osiewacz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003300:Copper / Q000378:metabolism*; D004271:DNA, Fungal; D003576:Electron Transport Complex IV / Q000378:metabolism; D005656:Fungal Proteins; D015870:Gene Expression; D005800:Genes, Fungal; D006801:Humans; D007501:Iron / Q000378:metabolism; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000378:metabolism; D010940:Plant Proteins; D017386:Sequence Homology, Amino Acid; D020037:Sordariales / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D013482:Superoxide Dismutase / Q000235:genetics / Q000378:metabolism*; D000072105:Superoxide Dismutase-1; D014157:Transcription Factors / Q000235:genetics; D000099188:Alternative Oxidase; D000099156:Superoxide Dismutase 2
chemical_list: D003300:Copper; D004271:DNA, Fungal; D003576:Electron Transport Complex IV; D005656:Fungal Proteins; D007501:Iron; D024101:Mitochondrial Proteins; D010088:Oxidoreductases; D010940:Plant Proteins; D013482:Superoxide Dismutase; D000072105:Superoxide Dismutase-1; D014157:Transcription Factors; D000099188:Alternative Oxidase; D000099156:Superoxide Dismutase 2; C101526:GRISEA protein, Podospora anserina; C000606290:SOD1 protein, human