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Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
Open accessAbstract
Calorie restriction extends lifespan in a broad range of organisms, from yeasts to mammals. Numerous hypotheses have been proposed to explain this phenomenon, including decreased oxidative damage and altered energy metabolism. In Saccharomyces cerevisiae, lifespan extension by calorie restriction requires the NAD+-dependent histone deacetylase, Sir2 (ref. 1). We have recently shown that Sir2 and its closest human homologue SIRT1, a p53 deacetylase, are strongly inhibited by the vitamin B3 precursor nicotinamide. Here we show that increased expression of PNC1 (pyrazinamidase/nicotinamidase 1), which encodes an enzyme that deaminates nicotinamide, is both necessary and sufficient for lifespan extension by calorie restriction and low-intensity stress. We also identify PNC1 as a longevity gene that is responsive to all stimuli that extend lifespan. We provide evidence that nicotinamide depletion is sufficient to activate Sir2 and that this is the mechanism by which PNC1 regulates longevity. We conclude that yeast lifespan extension by calorie restriction is the consequence of an active cellular response to a low-intensity stress and speculate that nicotinamide might regulate critical cellular processes in higher organisms.
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“Several studies highlight how the external environment and the genetic background of an organism have pivotal roles in the aging process by affecting events that maintain epigenetic information 2,3 .”
From Mechanisms, pathways and strategies for rejuvenation through epigenetic reprogramming (2023) · cites this paper as [3]
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“NAM, in contrast, is a well reported and widely used sirtuin inhibitor31 and has been recently shown to inhibit NAD+-consuming activities in vivo24.”
From NRK1 controls nicotinamide mononucleotide and nicotinamide riboside metabolism in mammalian cells (2016) · cites this paper as [31]
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“In response to calorie restriction, the yeast NAD biosynthetic gene that catalyses the first and rate-limiting step in NAD+ biosynthesis, PNC1, is induced46.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [46]
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“The resulting availability of NAD+ increases SIR2 activity, which boosts mitochondrial respiration and suppresses recombinant DNA recombination11,46, a known cause of ageing in yeast47.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [46]
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“The upregulation of the NAD salvage pathway, which recycles NAD+ from nicotinamide, was first shown to extend lifespan and mimic caloric restriction in yeast cells46.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [46]
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Genomic Expression Programs in the Response of Yeast Cells to Environmental Changes
Gasch, A. P., Spellman, P. T., Kao, C. M., Carmel-Harel, O., Eisen, M. B., Storz, G., Botstein, D., & Brown, P. O. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.12.4241 · Cited by 4,815
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
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · cited 1×
“Cells with an additional copy of SIR2 live 30% longer than the wild type, whereas sir2Δ strains age prematurel”
BackgroundNegative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
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
Extrachromosomal rDNA circles—a cause of aging in yeast
Sinclair, D. A., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80493-6 · Cited by 1,500
Self-citationThe Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors
Virág, L., & Szabó, C. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.375 · Cited by 1,373
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
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Petrossian, T. C., & Clarke, S. G. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.000976 · Cited by 304
Strategies for Reducing or Preventing the Generation of Oxidative Stress
Poljšak, B. (2011) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2011/194586 · Cited by 299
Hsu, C., Oka, S., Shao, D., Hariharan, N., & Sadoshima, J. (2009) · Circulation Research · doi:10.1161/circresaha.109.203703 · Cited by 289
Anderson, R. M., Barger, J. L., Edwards, M. G., Braun, K. H., O’Connor, C. E., Prolla, T. A., & Weindruch, R. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2007.00357.x · Cited by 283
“For example, in yeast, CR and numerous low-intensity stressors associated with longevity acti- vate a common pathway to influence lifespan (Anderson et al., 2003).”
BackgroundSelf-citationCalorie Restriction: Is AMPK a Key Sensor and Effector
Cantó, C., & Auwerx, J. (2011) · Physiology · doi:10.1152/physiol.00010.2011 · Cited by 282
Nitric oxide and mitochondrial biogenesis
Nisoli, E., & Carruba, M. O. (2006) · Journal of Cell Science · doi:10.1242/jcs.03062 · Cited by 285
Replicative Aging in Yeast: The Means to the End
Steinkraus, K. A., Kaeberlein, M. R., & Kennedy, B. K. (2008) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123509 · Cited by 282
Braidy, N., Berg, J., Clement, J., Khorshidi, F., Poljak, A., Jayasena, T., Grant, R., & Sachdev, P. S. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7269 · Cited by 294
Torres, N., Guevara‐Cruz, M., Velázquez‐Villegas, L. A., & Tovar, A. R. (2015) · Archives of Medical Research · doi:10.1016/j.arcmed.2015.05.010 · Cited by 289
Lifespan and healthspan extension by resveratrol
Bhullar, K. S., & Hubbard, B. P. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.01.012 · Cited by 278
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Jing, H., & Lin, H. (2015) · Chemical Reviews · doi:10.1021/cr500457h · Cited by 276
Lezon, T. R., Banavar, J. R., Cieplak, M., Maritan, A., & Fedoroff, N. V. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609152103 · Cited by 266
NAD metabolism: Implications in aging and longevity
Yaku, K., Okabe, K., & Nakagawa, T. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.05.006 · Cited by 269
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Hursting, S. D., & Berger, N. A. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2010.27.9935 · Cited by 257
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Anderson, K. A., & Hirschey, M. D. (2012) · Essays in Biochemistry · doi:10.1042/bse0520023 · Cited by 249
Global heterochromatin loss: a unifying theory of aging?
Tsurumi, A., & Li, W. (2012) · Epigenetics · doi:10.4161/epi.20540 · Cited by 256
Wang, B., Hasan, M. K., Alvarado, E., Yuan, H., Wu, H., & Chen, W. (2010) · Oncogene · doi:10.1038/onc.2010.468 · Cited by 250
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Jackson, M. D., Schmidt, M. T., Oppenheimer, N. J., & Denu, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306552200 · Cited by 240
Satoh, A., Brace, C. S., Ben-Josef, G., West, T., Wozniak, D. F., Holtzman, D. M., Herzog, E. D., & Imai, S.-I. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1385-10.2010 · Cited by 237
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Schmeisser, K., Mansfeld, J., Kuhlow, D., Weimer, S., Priebe, S., Heiland, I., Birringer, M., Groth, M., Segref, A., Kanfi, Y., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1352 · Cited by 236
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Bitterman, K. J., Medvedik, O., & Sinclair, D. A. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.3.376-399.2003 · Cited by 240
Self-citationMicroReview: Small molecules that regulate lifespan: evidence for xenohormesis
Lamming, D. W., Wood, J. G., & Sinclair, D. A. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04209.x · Cited by 232
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Lamming, D. W., Latorre‐Esteves, M., Medvedik, O., Wong, S. N., Tsang, F. A., Wang, C., Lin, S.-J., & Sinclair, D. A. (2005) · Science · doi:10.1126/science.1113611 · Cited by 227
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Sinclair, D. A., & Guarente, L. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134657 · Cited by 226
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Zorn, J. A., & Wells, J. A. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.318 · Cited by 222
Smith, D. L., McClure, J. M., Matecic, M., & Smith, J. S. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00326.x · Cited by 225
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Pan, H., & Finkel, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.771915 · Cited by 228
Kohlwein, S. D., Marten Veenhuis, A., & van der Klei, I. J. (2012) · Genetics · doi:10.1534/genetics.112.143362 · Cited by 213
Curtis, R., O'Connor, G., & DiStefano, P. S. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00205.x · Cited by 220
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Newman, J. C., He, W., & Verdin, E. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.404863 · Cited by 210
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Merry, B. J. (2003) · Aging Cell · doi:10.1046/j.1474-9728.2003.00074.x · Cited by 207
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Boo, Y. C. (2021) · Antioxidants · doi:10.3390/antiox10081315 · Cited by 225
Imai, S. (2009) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-008-9041-4 · Cited by 203
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Wang, H., Kazemi‐Esfarjani, P., & Benzer, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404648101 · Cited by 198
Wei, M., Fabrizio, P., Madia, F., Hu, J. H., Ge, H., Li, L. M., & Longo, V. D. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000467 · Cited by 196
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Yu, J., & Auwerx, J. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04952.x · Cited by 145
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Gallo, C. M., Smith, D. L., & Smith, J. S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.1301-1312.2004 · Cited by 193
Koç, A., Gasch, A. P., Rutherford, J. C., Kim, H., & Gladyshev, V. N. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307929101 · Cited by 192
Jeninga, E. H., Schoonjans, K., & Auwerx, J. H. (2010) · Oncogene · doi:10.1038/onc.2010.206 · Cited by 197
Janke, R., Dodson, A. E., & Rine, J. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100814-125544 · Cited by 199
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Kaeberlein, M. R., Hu, D., Kerr, E. O., Tsuchiya, M., Westman, E. A., Dang, N., Fields, S., & Kennedy, B. K. (2005) · PLoS Genetics · doi:10.1371/journal.pgen.0010069 · Cited by 193
Zhang, X., Ji, R., Liao, X., Castillero, E., Kennel, P. J., Brunjes, D. L., Franz, M., Möbius‐Winkler, S., Drosatos, K., George, I., et al. (2018) · Circulation · doi:10.1161/circulationaha.117.030486 · Cited by 187
van der Veer, E., Nong, Z., O’Neil, C. H., Urquhart, B. L., Freeman, D. J., & Pickering, J. G. (2005) · Circulation Research · doi:10.1161/01.res.0000173298.38808.27 · Cited by 189
Zhao, K., Harshaw, R. B., Chai, X., & Marmorstein, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401057101 · Cited by 186
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Chen, D., & Guarente, L. (2007) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.12.004 · Cited by 187
Soanes, D. M., Alam, I. S., Cornell, M., Wong, H. M., Hedeler, C., Paton, N. W., Rattray, M., Hubbard, S. J., Oliver, S. G., & Talbot, N. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002300 · Cited by 184
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Capello, M., Borgogno, S. F., Riganti, C., Chattaragada, M. S., Principe, M., Roux, C., Zhou, W., Petricoin, E. F., Cappello, P., & Novelli, F. (2015) · Oncotarget · doi:10.18632/oncotarget.6798 · Cited by 153
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Avalos, J. L., Boeke, J. D., & Wolberger, C. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00082-6 · Cited by 153
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Katic, M., Kennedy, A. R., Leykin, I., Norris, A., McGettrick, A., Gesta, S., Russell, S. J., Bluher, M., Maratos‐Flier, E., & Kahn, C. R. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00346.x · Cited by 141
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Metadata
- Authors
- Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A.
- Affiliations
- Harvard University (US)
- Corresponding author
- Sinclair, David A.
- Venue
- Nature
- Published
- 2003-05
- Volume
- 423
- Issue
- 6936
- Pages
- 181-185
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC4802858
- OpenAlex
- W2006806054
- Cited by
- 736
- References
- 30
- Citations by year
- 2026: 18 · 2025: 17 · 2024: 11 · 2023: 10 · 2022: 26 · 2021: 18 · 2020: 24 · 2019: 23 · 2018: 30 · 2017: 26 · 2016: 29 · 2015: 35 · 2014: 30 · 2013: 24 · 2012: 39
- FWCI
- 13.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute on Aging (R37AG028730, P01AG027916, R01AG028730, R01AG019719, R01AG019972)
- National Institute of General Medical Sciences (R01GM068072)
- 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, lifespan extension, nicotinamide, Sir2, SIRT1, NAD+-dependent histone deacetylase, longevity genes, Saccharomyces cerevisiae, aging
- MeSH terms
- Cell Nucleus, Cytoplasm, Energy Metabolism, Histone Deacetylases, Longevity, NAD, Niacin, Nicotinamidase, Niacinamide, Saccharomyces cerevisiae, Gene Expression Regulation, Fungal, Heat-Shock Response, Gene Silencing, Saccharomyces cerevisiae Proteins, Caloric Restriction, Sirtuins, Silent Information Regulator Proteins, Saccharomyces cerevisiae, Sirtuin 2
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