Cited by 632Genetics, Aging, and Longevity in Model OrganismsSirtuins and Resveratrol in MedicineFungal and yeast genetics research

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Calorie restriction extends yeast life span by lowering the level of NADH

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Lin, Su-Ju, Ford, Ethan, Haigis, Marcia, Liszt, Greg, Guarente, Leonard·2004·Genes & Development

DOI 10.1101/gad.1164804PMC PMC314267

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Abstract

Calorie restriction (CR) extends life span in a wide variety of species. Previously, we showed that calorie restriction increases the replicative life span in yeast by activating Sir2, a highly conserved NAD-dependent deacetylase. Here we test whether CR activates Sir2 by increasing the NAD/NADH ratio or by regulating the level of nicotinamide, a known inhibitor of Sir2. We show that CR decreases NADH levels, and that NADH is a competitive inhibitor of Sir2. A genetic intervention that specifically decreases NADH levels increases life span, validating the model that NADH regulates yeast longevity in response to CR.

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Methods in yeast genetics
Sherman, F., Fink, G. R., & Hicks, J. B. (1979) · Cold Spring Harbor Laboratory eBooks · Cited by 7,430
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
Self-citation
The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
Self-citation
Requirement of NAD and SIR2 for Life-Span Extension by Calorie Restriction in Saccharomyces cerevisiae
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
Self-citation
A new efficient gene disruption cassette for repeated use in budding yeast
Güldener, U. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.13.2519 · Cited by 1,657
Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,603
Self-citation
Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
Lin, S.-J., Kaeberlein, M., Andalis, A. A., Sturtz, L. A., Defossez, P.-A., Culotta, V. C., Fink, G. R., & Guarente, L. (2002) · Nature · doi:10.1038/nature00829 · Cited by 1,057
Self-citation
Inhibition of Silencing and Accelerated Aging by Nicotinamide, a Putative Negative Regulator of Yeast Sir2 and Human SIRT1
Bitterman, K. J., Anderson, R. M., Cohen, H. Y., Latorre-Esteves, M., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205670200 · Cited by 1,002
The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., & Sternglanz, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110148297 · Cited by 970
Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736

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Sherman F . 2002. Guide to yeast genetics and molecular and cellular biology. In Methods in enzymology (eds. C. Guthrie and G.R. Fink), pp. 3–41. Academic Press, San Diego.

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Authors: Lin, S.-J., Ford, E., Haigis, M., Liszt, G., & Guarente, L.
Affiliations: Massachusetts Institute of Technology (US)
ORCID: Lin, Su-Ju
Ford, Ethan
Haigis, Marcia
Guarente, Leonard
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 2004-01-01
Volume: 18
Issue: 1
Pages: 12-16
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.1164804
PMC: PMC314267
OpenAlex: W2136829516
Cited by: 632
References: 31
Citations by year: 2026: 8 · 2025: 6 · 2024: 11 · 2023: 11 · 2022: 8 · 2021: 25 · 2020: 20 · 2019: 17 · 2018: 34 · 2017: 20 · 2016: 32 · 2015: 33 · 2014: 35 · 2013: 36 · 2012: 36
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genes & Development (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Ellison Medical Foundation
National Institutes of Health
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 › Molecular Biology › Fungal and yeast genetics research
Keywords: caloric restriction, replicative lifespan, Sir2, NADH, NAD+/NADH ratio, nicotinamide, NAD+-dependent deacetylase, yeast longevity, competitive inhibition
MeSH terms: Culture Media, NAD, Oxidation-Reduction, Saccharomyces cerevisiae, Sirtuins

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Calorie restriction extends yeast life span by lowering the level of NADH

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