Cited by 238Genetics, Aging, and Longevity in Model OrganismsSirtuins and Resveratrol in MedicineAutophagy in Disease and Therapy

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Role of sirtuins in lifespan regulation is linked to methylation of nicotinamide

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Schmeisser, Kathrin, Mansfeld, Johannes, Kuhlow, Doreen, Weimer, Sandra, Priebe, Steffen, Heiland, Ines, Birringer, Marc, Groth, Marco, Segref, Alexandra, Kanfi, Yariv, Price, Nathan L, Schmeisser, Sebastian, Schuster, Stefan, Pfeiffer, Andreas F H, Guthke, Reinhard, Platzer, Matthias, Hoppe, Thorsten, Cohen, Haim Y, Zarse, Kim, Sinclair, David A, Ristow, Michael·2013·Nature Chemical Biology

DOI 10.1038/nchembio.1352PMC PMC4076143

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Abstract

Sirtuins, a family of histone deacetylases, have a fiercely debated role in regulating lifespan. In contrast with recent observations, here we find that overexpression of sir-2.1, the ortholog of mammalian SirT1, does extend Caenorhabditis elegans lifespan. Sirtuins mandatorily convert NAD(+) into nicotinamide (NAM). We here find that NAM and its metabolite, 1-methylnicotinamide (MNA), extend C. elegans lifespan, even in the absence of sir-2.1. We identify a previously unknown C. elegans nicotinamide-N-methyltransferase, encoded by a gene now named anmt-1, to generate MNA from NAM. Disruption and overexpression of anmt-1 have opposing effects on lifespan independent of sirtuins, with loss of anmt-1 fully inhibiting sir-2.1-mediated lifespan extension. MNA serves as a substrate for a newly identified aldehyde oxidase, GAD-3, to generate hydrogen peroxide, which acts as a mitohormetic reactive oxygen species signal to promote C. elegans longevity. Taken together, sirtuin-mediated lifespan extension depends on methylation of NAM, providing an unexpected mechanistic role for sirtuins beyond histone deacetylation.

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Authors: Schmeisser, K., Mansfeld, J., Kuhlow, D., Weimer, S., Priebe, S., Heiland, I., Birringer, M., Groth, M., Segref, A., Kanfi, Y., Price, N. L., Schmeisser, S., Schuster, S., Pfeiffer, A. F. H., Guthke, R., Platzer, M., Hoppe, T., Cohen, H. Y., Zarse, K., Sinclair, D. A., & Ristow, M.
Affiliations: Friedrich Schiller University Jena (DE)
ETH Zurich (CH)
German Institute of Human Nutrition (DE)
Fulda University of Applied Sciences (DE)
Leibniz Institute on Aging - Fritz Lipmann Institute (FLI) (DE)
University of Cologne (DE)
Bar-Ilan University (IL)
Harvard University (US)
Leibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) (DE)
Corresponding author: Ristow, Michael
ORCID: Schmeisser, Kathrin
Heiland, Ines
Birringer, Marc
Groth, Marco
Segref, Alexandra
Price, Nathan L
Schmeisser, Sebastian
Schuster, Stefan
Pfeiffer, Andreas F H
Platzer, Matthias
Hoppe, Thorsten
Cohen, Haim Y
Zarse, Kim
Sinclair, David A
Ristow, Michael
Venue: Nature Chemical Biology
Publisher: Springer Science and Business Media LLC
Published: 2013-09-29
Volume: 9
Issue: 11
Pages: 693-700
ISSN: 1552-4450 (ISSN-L)
1552-4469
DOI: 10.1038/nchembio.1352
PMC: PMC4076143
OpenAlex: W1974979950
Cited by: 236
References: 56
Citations by year: 2026: 2 · 2025: 12 · 2024: 14 · 2023: 14 · 2022: 25 · 2021: 20 · 2020: 27 · 2019: 18 · 2018: 17 · 2017: 15 · 2016: 20 · 2015: 27 · 2014: 22 · 2013: 3
FWCI: 8.63
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature Chemical Biology (publishedVersion)
PubMed (publishedVersion)
Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (P40OD010440)
National Institute on Aging (R37AG028730)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: sirtuins, SIRT1, sir-2.1, lifespan extension, Caenorhabditis elegans, nicotinamide, N1-methylnicotinamide, nicotinamide N-methyltransferase, aldehyde oxidase, hydrogen peroxide, mitohormesis, reactive oxygen species signaling, NAD+ metabolism, longevity
MeSH terms: Animals, Longevity, Methylation, Niacinamide, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Sirtuins

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Role of sirtuins in lifespan regulation is linked to methylation of nicotinamide

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