The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress.
PaMTH1 is an O-methyltransferase catalysing the methylation of vicinal hydroxyl groups of polyphenols. The protein accumulates during ageing of Podospora anserina in both the cytosol and in the mitochondrial matrix. The construction and characterisation of a PaMth1 deletion strain provided additional evidence about the function of the protein in the protection against metal induced oxidative stress. Deletion of PaMth1 was found to lead to a decreased resistance against exogenous oxidative stress and to a shortened lifespan suggesting a role of PaMTH1 as a longevity assurance factor in a new molecular pathway involved in lifespan control.
Department of Biological Sciences & Cluster of Excellence Macromolecular Complexes, Institute of Molecular Biosciences, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany.
Birgit
B
Kunstmann
Heinz D
HD
Osiewacz
D019327:Copper Sulfate / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology; D005656:Fungal Proteins / Q000502:physiology*; D017353:Gene Deletion; D006861:Hydrogen Peroxide / Q000378:metabolism; D053858:Metabolic Networks and Pathways; D008780:Methyltransferases / Q000502:physiology*; D008928:Mitochondria / Q000201:enzymology; D018384:Oxidative Stress; D048468:Podospora / Q000737:chemistry / Q000201:enzymology* / Q000254:growth & development*; D017382:Reactive Oxygen Species
D005656:Fungal Proteins; D017382:Reactive Oxygen Species; D006861:Hydrogen Peroxide; D008780:Methyltransferases; C409687:PaMTH1 protein, Podospora anserina; D019327:Copper Sulfate