title: Over-expression of an S-adenosylmethionine-dependent methyltransferase leads to an extended lifespan of Podospora anserina without impairments in vital functions.
abstract: PaMTH1, a putative methyltransferase previously described to increase in abundance in total protein extracts during aging of Podospora anserina is demonstrated to accumulate in the mitochondrial cell fraction of senescent cultures. The protein is localized in the mitochondrial matrix and displays a methyltransferase activity utilizing flavonoids as substrates. Constitutive over-expression of PaMth1 in P. anserina results in a reduced carbonylation of proteins and an extended lifespan without impairing vital functions suggesting a protecting role of PaMTH1 against oxidative stress.
authors.affiliation: Department of Biological Sciences & Cluster of Excellence Macromolecular Complexes, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt, Frankfurt am Main, Germany.
authors.forename: Birgit
authors.initials: B
authors.lastname: Kunstmann
authors.forename: Heinz D
authors.initials: HD
authors.lastname: Osiewacz
mesh_terms: D000818:Animals; D005656:Fungal Proteins / Q000096:biosynthesis* / Q000145:classification / Q000235:genetics* / Q000502:physiology; D015966:Gene Expression Regulation, Fungal / Q000502:physiology*; D006801:Humans; D008780:Methyltransferases / Q000096:biosynthesis* / Q000145:classification / Q000235:genetics* / Q000502:physiology; D024101:Mitochondrial Proteins / Q000096:biosynthesis / Q000145:classification / Q000235:genetics / Q000502:physiology; D018384:Oxidative Stress / Q000235:genetics / Q000502:physiology; D048468:Podospora / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development* / Q000502:physiology; D051381:Rats; D012436:S-Adenosylmethionine / Q000502:physiology*; D013997:Time Factors
chemical_list: D005656:Fungal Proteins; D024101:Mitochondrial Proteins; D012436:S-Adenosylmethionine; D008780:Methyltransferases; C409687:PaMTH1 protein, Podospora anserina