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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]
In the citing paper
“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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Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes
Sanders, B. D., Zhao, K., Slama, J. T., & Marmorstein, R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.022 · Cited by 68
Benayoun, B. A., Batista, F., Auer, J., Dipietromaria, A., L’Hôte, D., Baere, E. B. W. D., & Veitia, R. A. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn389 · Cited by 70
Role of sirtuins, calorie restriction and physical activity in aging
Corbi, G. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/417 · Cited by 66
Mechanisms, pathways and strategies for rejuvenation through epigenetic reprogramming
Cipriano, A., Moqri, M., Maybury-Lewis, S. Y., Rogers-Hammond, R., de Jong, T. A., Parker, A., Rasouli, S., Schöler, H. R., Sinclair, D. A., & Sebastiano, V. (2023) · Nature Aging · doi:10.1038/s43587-023-00539-2 · Cited by 66
Self-citationNAD: A master regulator of transcription
Ghosh, S., George, S., Roy, U., Ramachandran, D., & Kolthur‐Seetharam, U. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.08.002 · Cited by 64
Xu, J., Capezzone, M., Xu, X. L., & Hershman, J. M. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0215 · Cited by 65
Sirtuins (histone deacetylases III) in the cellular response to DNA damage—Facts and hypotheses
Kruszewski, M. K., & Szumiel, I. (2005) · DNA repair · doi:10.1016/j.dnarep.2005.06.013 · Cited by 65
Bogan, K. L., Evans, C., Belenky, P., Song, P., Burant, C. F., Kennedy, R., & Brenner, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.056689 · Cited by 63
Resveratrol inhibits proliferation and promotes apoptosis of osteosarcoma cells
Li, Y., Bäckesjö, C., Haldosén, L.-A., & Lindgren, U. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.03.004 · Cited by 61
Systemic regulation of mammalian ageing and longevity by brain sirtuins
Satoh, A., & Imai, S. (2014) · Nature Communications · doi:10.1038/ncomms5211 · Cited by 63
Madsen, C. T., Sylvestersen, K. B., Young, C., Buch-Larsen, S. C., Poulsen, J. W., Agerholm, M., Palmqvist, E. A., Hey‐Mogensen, M., Jensen, P. B., Treebak, J. T., et al. (2015) · Nature Communications · doi:10.1038/ncomms8726 · Cited by 61
Qiao, A., Jin, X., Pang, J., Moskophidis, D., & Mivechi, N. F. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201607091 · Cited by 65
Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein
Zheng, X., Dai, X., Zhao, Y., Chen, Q., Lu, F., Yao, D., Yu, Q., Liu, X., Zhang, C., Gu, X., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700480104 · Cited by 62
Diversification of NAD biological role : the importance of location
Stefano, M. D., & Conforti, L. (2013) · FEBS Journal · doi:10.1111/febs.12433 · Cited by 62
Swain, S., Wren, J. F., Stürzenbaum, S. R., Kille, P., Morgan, A. J., Jager, T., Jonker, M. J., Hankard, P. K., Svendsen, C., Owen, J., et al. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-32 · Cited by 69
Navigating novel mechanisms of cellular plasticity with the NAD+ precursor and nutrient nicotinamide
Li, F. (2004) · Frontiers in bioscience · doi:10.2741/1412 · Cited by 61
Hashimoto, T., Horikawa, M., Nomura, T., & Sakamoto, K. (2009) · Biogerontology · doi:10.1007/s10522-009-9225-3 · Cited by 63
Hong, E., Yun, H. S., Kim, J., Um, H., Lee, K.-H., Kang, C., Lee, S., Chun, J., & Hwang, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.219832 · Cited by 60
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Suzuki, T., Imai, K., Nakagawa, H., & Miyata, N. (2006) · ChemMedChem · doi:10.1002/cmdc.200600162 · Cited by 60
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Wong, S. Y., & Tang, B. L. (2016) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0023 · Cited by 59
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Wang, T., Tseng, W.-C., Leu, Y., Chen, C., Chi, Y.-C., Chi, Y.-C., Cheng, S.-F., Lai, C.-Y., Kuo, C.-H., Yang, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28908-2 · Cited by 61
Unraveling Parkinson’s Disease Neurodegeneration: Does Aging Hold the Clues?
Coleman, C., & Martin, I. (2022) · Journal of Parkinson s Disease · doi:10.3233/jpd-223363 · Cited by 65
Dal‐Pan, A., Terrien, J., Pifferi, F., Botalla, R., Hardy, I., Marchal, J., Zahariev, A., Chery, I., Zizzari, P., Perret, M., et al. (2010) · AGE · doi:10.1007/s11357-010-9156-6 · Cited by 65
Włodarski, T., Kutner, J., Towpik, J., Kniżewski, Ł., Rychlewski, L., Kudlicki, A. S., Rowicka, M., Dziembowski, A., & Ginalski, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023168 · Cited by 58
French, J. B., Cen, Y., Vrablik, T. L., Xu, P., Allen, E. K. H., Hanna‐Rose, W., & Sauve, A. A. (2010) · Biochemistry · doi:10.1021/bi1012518 · Cited by 59
NAD+ Metabolism and Regulation: Lessons From Yeast
Croft, T., Venkatakrishnan, P., & Lin, S.-J. (2020) · Biomolecules · doi:10.3390/biom10020330 · Cited by 62
Yeast as a model to study mitochondrial mechanisms in ageing
de Barros, M. H., da Cunha, F. M., de Oliveira, G. A., Tahara, E. B., & Kowaltowski, A. J. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.04.008 · Cited by 58
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Zhang, S., Cai, G., Fu, B., Feng, Z., Ding, R., Bai, X., Liu, W., Zhuo, L., Sun, L., Liu, F., et al. (2012) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2012.04.005 · Cited by 57
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Wuttke, D., Connor, R. A., Vora, C., Craig, T., Li, Y., Wood, S. H., Vasieva, O., Reis, R. J. S., Tang, F., & de Magalhães, J. P. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002834 · Cited by 55
Pagliassotti, M. J., Estrada, A. L., Hudson, W. M., Wei, Y., Wang, D., Seals, D. R., Zigler, M. L., & LaRocca, T. J. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2017.02.022 · Cited by 58
Characterization of Nuclear Sirtuins: Molecular Mechanisms and Physiological Relevance
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Aerts, A., François, I., Bammens, L., Cammue, B. P. A., Smets, B., Winderickx, J., Accardo, S., Vos, D. E. D., & Thevissen, K. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.02.061 · Cited by 57
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Banerjee, K. K., Ayyub, C., Sengupta, S., & Kolthur‐Seetharam, U. (2012) · Aging · doi:10.18632/aging.100435 · Cited by 54
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Imai, S. (2009) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32832c932d · Cited by 55
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Wu, L., Ren, D., Hu, S., Li, G., Dong, G., Jiang, L., Hu, X., Ye, W., Cui, Y., Zhu, L., et al. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.01898 · Cited by 55
The NAD+ precursor nicotinamide riboside decreases exercise performance in rats
Kourtzidis, I. A., Stoupas, A. T., Gioris, I. S., Veskoukis, A. S., Margaritelis, N. V., Tsantarliotou, M. P., Taitzoglou, I., Vrabas, I. S., Paschalis, V., Kyparos, A., et al. (2016) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-016-0143-x · Cited by 55
Wang, X., He, H., Xiong, X., Zhou, S., Wang, W., Feng, L., Han, R., & Xie, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.668491 · Cited by 56
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Hunt, N. D., Hyun, D., Allard, J. S., Minor, R. K., Mattson, M. P., Ingram, D. K., & de Cabo, R. (2006) · Ageing Research Reviews · doi:10.1016/j.arr.2006.03.006 · Cited by 55
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Wang, T., Geng, S., Guan, Y.-M., & Xu, W. (2018) · Aging · doi:10.18632/aging.101447 · Cited by 54
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Kennedy, B. K., & Kaeberlein, M. R. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00522.x · Cited by 54
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van der Horst, A., Schavemaker, J. M., Berkel, W. P.-V., & Burgering, B. M. T. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.01.004 · Cited by 53
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Yu, M. C., Lamming, D. W., Eskin, J. A., Sinclair, D. A., & Silver, P. A. (2006) · Genes & Development · doi:10.1101/gad.1495206 · Cited by 57
Self-citationChen, Y., Jiang, Y., Yang, Y., Huang, X., & Sun, C. (2021) · Neurotoxicity Research · doi:10.1007/s12640-021-00392-4 · Cited by 53
Easlon, E. J., Tsang, F. A., Dilova, I., Wang, C., Lu, S.-P., Skinner, C., & Lin, S.-J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607661200 · Cited by 55
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Effelsberg, D., Cruz‐Zaragoza, L. D., Tonillo, J., Schliebs, W., & Erdmann, R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.653451 · Cited by 52
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Vendrell, A., Martínez-Pastor, M., González‐Novo, A., Pascual‐Ahuir, A., Sinclair, D. A., Proft, M., & Posas, F. (2011) · EMBO Reports · doi:10.1038/embor.2011.154 · Cited by 52
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Huberts, D. H. E. W., González, J., Lee, S. S., Litsios, A., Hubmann, G., Wit, E. C., & Heinemann, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410024111 · Cited by 60
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Breitenbach, M., Laun, P., & Jazwinski, S. M. (2011) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-2561-4 · Cited by 55
Vrablik, T. L., Huang, L., Lange, S. E., & Hanna‐Rose, W. (2009) · Development · doi:10.1242/dev.028431 · Cited by 49
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Ocampo, A., Liu, J., & Barrientos, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt016 · Cited by 47
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Saini, A. S., Al‐Shanti, N., Sharples, A. P., & Stewart, C. E. (2011) · Experimental Physiology · doi:10.1113/expphysiol.2011.061028 · Cited by 44
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Rahman, M. M., Halade, G. V., Bhattacharya, A., & Fernandes, G. (2009) · Oxidative Medicine and Cellular Longevity · doi:10.4161/oxim.2.5.9579 · Cited by 48
Belenky, P. A., Stebbins, R. C., Bogan, K. L., Evans, C. R., & Brenner, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019710 · Cited by 43
Orlandi, I., Alberghina, L., & Vai, M. (2020) · Biomolecules · doi:10.3390/biom10040604 · Cited by 40
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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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