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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 additiona...

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Detalles Bibliográficos
Autores principales: Kunstmann, Birgit, Osiewacz, Heinz D.
Formato: Texto
Lenguaje:English
Publicado: Impact Journals LLC 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2806012/
https://www.ncbi.nlm.nih.gov/pubmed/20157520
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author Kunstmann, Birgit
Osiewacz, Heinz D.
author_facet Kunstmann, Birgit
Osiewacz, Heinz D.
author_sort Kunstmann, Birgit
collection PubMed
description 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.
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spelling pubmed-28060122010-02-12 The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress Kunstmann, Birgit Osiewacz, Heinz D. Aging (Albany NY) Research Article 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. Impact Journals LLC 2009-03-03 /pmc/articles/PMC2806012/ /pubmed/20157520 Text en Copyright: ©2009 Kunstmann et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Kunstmann, Birgit
Osiewacz, Heinz D.
The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress
title The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress
title_full The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress
title_fullStr The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress
title_full_unstemmed The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress
title_short The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress
title_sort s-adenosylmethionine dependent o-methyltransferase pamth1: a longevity assurance factor protecting podospora anserina against oxidative stress
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2806012/
https://www.ncbi.nlm.nih.gov/pubmed/20157520
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