Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
Open accessAbstract
We investigated the role of SIRT7, one of the seven members of the mammalian sirtuin family. We show that SIRT7 is a widely expressed nucleolar protein that is associated with active rRNA genes (rDNA), where it interacts with RNA polymerase I (Pol I) as well as with histones. Overexpression of SIRT7 increases Pol I-mediated transcription, whereas knockdown of SIRT7 or inhibition of the catalytic activity results in decreased association of Pol I with rDNA and a reduction of Pol I transcription. Depletion of SIRT7 stops cell proliferation and triggers apoptosis. Our findings suggest that SIRT7 is a positive regulator of Pol I transcription and is required for cell viability in mammals.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
SIRT7 appears necessary for preserving active rDNA transcription under conditions of cellular growth and stress.
“In contrast to the broadly repressive actions often attributed to other sirtuins, SIRT7 appears necessary for preserving active rDNA transcription under conditions of cellular growth and stress [183,184].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [183]
In “SIRT7 activates Pol I transcription” (page not provided), SIRT7 knockdown reduces pre-rRNA synthesis and Pol I association with rDNA; the paper also links SIRT7 activity to cell growth. It does not show that SIRT7 preserves active rDNA transcription under stress conditions. Its discussion of starvation and DNA damage describes effects on pre-rRNA synthesis generally, not a demonstrated protective role for SIRT7. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
A System for Stable Expression of Short Interfering RNAs in Mammalian Cells
Brummelkamp, T. R., Bernards, R., & Agami, R. (2002) · Science · doi:10.1126/science.1068999 · Cited by 4,295 · see citing works
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works
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 2,653 · see citing works
Self-citationKaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · cited 1× · see citing works
“In yeast, Sir2p promotes longevity predominantly through its silencing role at the rDNA (Sinclair and Guarente 1997; Kaeberlein et al. 1999).”
BackgroundSelf-citationGenomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6
Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637 · see citing works
Self-citationThe Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542 · see citing works
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 · see citing works
Self-citationThe Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,480 · see citing works
Self-citationPhylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409 · see citing works
Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., & Horikawa, I. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0033 · Cited by 1,364 · see citing works
Frye, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0897 · Cited by 809 · see citing works
Calorie restriction extends yeast life span by lowering the level of NADH
Lin, S.-J., Ford, E., Haigis, M., Liszt, G., & Guarente, L. (2004) · Genes & Development · doi:10.1101/gad.1164804 · Cited by 632 · see citing works
Self-citationSir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State
Fulco, M., Schiltz, R. L., Iezzi, S., King, M. T., Zhao, P., Kashiwaya, Y., Hoffman, E. P., Veech, R. L., & Sartorelli, V. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00226-0 · Cited by 581 · see citing works
Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase
Liszt, G., Ford, E., Kurtev, M., & Guarente, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413296200 · Cited by 548 · see citing works
Self-citationLife on a planet of its own: Regulation of RNA polymerase I transcription in the nucleolus
Grummt, I. (2003) · Genes & Development · doi:10.1101/gad.1098503r · Cited by 540 · see citing works
Self-citationGenetics and the Specificity of the Aging Process
Hekimi, S., & Guarente, L. (2003) · Science · doi:10.1126/science.1082358 · Cited by 434 · see citing works
Self-citationUse of Chromatin Immunoprecipitation To Clone Novel E2F Target Promoters
Weinmann, A. S., Bartley, S. M., Zhang, T., Zhang, M. Q., & Farnham, P. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.20.6820-6832.2001 · Cited by 381 · see citing works
The Sir2 family of protein deacetylases
Denu, J. M. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.08.010 · Cited by 325 · see citing works
Zhao, J., Yuan, X., Frödin, M., & Grummt, I. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00036-4 · Cited by 259 · see citing works
Self-citationYuan, X., Zhou, Y., Casanova, E., Chai, M., Kiss, É., Gröne, H., Schütz, G., & Grummt, I. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.05.023 · Cited by 250 · see citing works
Self-citationRegulation of Mammalian Ribosomal Gene Transcription by RNA Polymerase I
Grummt, I. (1998) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60506-1 · Cited by 237 · see citing works
Self-citationO’Sullivan, A., Sullivan, G. J., & McStay, B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.2.657-668.2002 · Cited by 215 · see citing works
Acetylation of TAFI68, a subunit of TIF‐IB/SL1, activates RNA polymerase I transcription
Muth, V., Nadaud, S., Grummt, I., & Voit, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1353 · Cited by 201 · see citing works
Self-citationPhosphorylation by G1‐specific cdk–cyclin complexes activates the nucleolar transcription factor UBF
Voit, R., Hoffmann, M., & Grummt, I. (1999) · The EMBO Journal · doi:10.1093/emboj/18.7.1891 · Cited by 181 · see citing works
Self-citationPercipalle, P., Fomproix, N., Cavellán, E., Voit, R., Reimer, G., Krüger, T., Thyberg, J., Scheer, U., Grummt, I., & Östlund Farrants, A. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400657 · Cited by 171 · see citing works
Self-citationKnuesel, M. T., Wan, Y., Xiao, Z., Holinger, E. P., Lowe, N., Wang, W., & Liu, X. (2003) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t300007-mcp200 · Cited by 122 · see citing works
Zatsepina, O. V., Voit, R., Grummt, I., et al. (1993) · Chromosoma · doi:10.1007/bf00352307 · Cited by 103 · see citing works
Self-citationConstitutive and strong association of PAF53 with RNA polymerase I
Seither, P., Zatsepina, O. V., Hoffmann, M., & Grummt, I. (1997) · Chromosoma · doi:10.1007/s004120050242 · Cited by 52 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K. 1997. Current protocols in molecular bi- ology. Wiley, New York.
- Percipalle, P., Fomproix, N., Cavellán, E., Voit, R., Reimer, G., Krüger, T., Thyberg, J., Scheer, U., Grummt, I., and Östlund-Farrants, A.-K. 2006. The chromain remodeling complex WSTF-SNH2g interacts with nuclear myosin 1 and serves a role in RNA polymerase I transcrip- tion. EMBO Rep. (in press).
Cited by
Sorted by citations
Reactive oxygen species, cellular redox systems, and apoptosis
Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340 · see citing works
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works
Ying, W. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1672 · Cited by 1,494 · see citing works
Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction
Haigis, M. C., & Guarente, L. P. (2006) · Genes & Development · doi:10.1101/gad.1467506 · Cited by 1,295 · see citing works
Self-citationHaigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162 · see citing works
Self-citationThe secret life of NAD+: an old metabolite controlling new metabolic signaling pathways
Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899 · see citing works
Sirtuin Functions in Health and Disease
Yamamoto, H., Schoonjans, K., & Auwerx, J. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0079 · Cited by 480 · see citing works
Sirtuins as potential targets for metabolic syndrome
Guarente, L. (2006) · Nature · doi:10.1038/nature05486 · Cited by 468 · see citing works
Self-citationSirtuins, a promising target in slowing down the ageing process
Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470 · see citing works
Sirtuins: The ‘ <i>magnificent seven</i> ’, function, metabolism and longevity
Dali‐Youcef, N., Lagouge, M., Froelich, S., Koehl, C., Schoonjans, K., & Auwerx, J. (2007) · Annals of Medicine · doi:10.1080/07853890701408194 · Cited by 402 · see citing works
Epigenetic control of rDNA loci in response to intracellular energy status
Murayama, A., Ohmori, K., Fujimura, A., Minami, H., Yasuzawa-Tanaka, K., Kuroda, T., Oie, S., Daitoku, H., Okuwaki, M., Nagata, K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.03.030 · Cited by 394 · see citing works
Redox control of senescence and age-related disease.
Chandrasekaran, A., Idelchik, M. D. P. S., & Melendez, J. A. (2017) · Redox Biology · doi:10.1016/j.redox.2016.11.005 · Cited by 360 · see citing works
SIRT7 represses Myc activity to suppress ER stress and prevent fatty liver disease
Shin, J., He, M., Liu, Y., Paredes, S., Villanova, L., Brown, K., Qiu, X., Nabavi, N., Mohrin, M., Wojnoonski, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.007 · Cited by 287 · see citing works
Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes
Cantó, C., Sauve, A. A., & Bai, P. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.004 · Cited by 246 · see citing works
Sirtuin regulation in aging and injury
Poulose, N., & Raju, R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.017 · Cited by 236 · see citing works
Huang, J.-Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.021 · Cited by 231 · see citing works
AMP-activated protein kinase adapts rRNA synthesis to cellular energy supply
Hoppe, S., Bierhoff, H., Cado, I., Weber, A., Tiebe, M., Grummt, I., & Voit, R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909873106 · Cited by 225 · see citing works
Self-citationKumar, V., Kundu, S., Singh, A., & Singh, S. (2022) · Current Neuropharmacology · doi:10.2174/1570159x19666210609160017 · Cited by 210 · see citing works
NAD <sup>+</sup> metabolism: A therapeutic target for age-related metabolic disease
Mouchiroud, L., Houtkooper, R. H., & Auwerx, J. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.789479 · Cited by 193 · see citing works
“No in vivo molecular deacetylation targets have been described for the nucleolar SIRT7, but knockdown or overexpression of SIRT7 resulted in decreased or increased RNA polymerase I-mediated transcription, respectively (Ford et al., 2006).”
BackgroundNAD+ biosynthesis, aging, and disease
Johnson, S., & Imai, S. (2018) · F1000Research · doi:10.12688/f1000research.12120.1 · Cited by 178 · see citing works
RETRACTED: Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex
Zhang, Q., Wang, S.-Y., Fleuriel, C., Leprince, D., Rocheleau, J. V., Piston, D. W., & Goodman, R. H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610590104 · Cited by 171 · see citing works
RetractedNAD<sup>+</sup>metabolism and oxidative stress: the golden nucleotide on a crown of thorns
Massudi, H., Grant, R., Guillemin, G. J., & Braidy, N. (2012) · Redox Report · doi:10.1179/1351000212y.0000000001 · Cited by 158 · see citing works
Chen, Q., Liu, Y., Ding, X., Li, Q., Qiu, F., Wang, M., Shen, Z., Zheng, H., & Fu, G. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-019-03671-z · Cited by 146 · see citing works
Alcaín, F. J., & Villalba, J. M. (2009) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543770902762893 · Cited by 137 · see citing works
Epigenetic control of RNA polymerase I transcription in mammalian cells
Grummt, I., & Längst, G. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.10.004 · Cited by 132 · see citing works
Self-citationSirtuin‐dependent epigenetic regulation in the maintenance of genome integrity
Bosch‐Presegué, L., & Vaquero, A. (2015) · The FEBS Journal · doi:10.1111/febs.13053 · Cited by 132 · see citing works
Blank, M. F., & Grummt, I. (2017) · Transcription · doi:10.1080/21541264.2016.1276658 · Cited by 111 · see citing works
HDAC8 cooperates with SMAD3/4 complex to suppress SIRT7 and promote cell survival and migration
Tang, X., Li, G., Su, F., Cai, Y., Shi, L., Meng, Y., Liu, Z., Sun, J., Wang, M., Qian, M., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa039 · Cited by 91 · see citing works
SIRT7 mediates L1 elements transcriptional repression and their association with the nuclear lamina
Vazquez, B. N., Thackray, J. K., Simonet, N. G., Chahar, S., Kane-Goldsmith, N., Newkirk, S. J., Lee, S., Xing, J., Verzi, M. P., An, W., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz519 · Cited by 79 · see citing works
Ha, C. W., & Huh, W.-K. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq895 · Cited by 77 · see citing works
Bao, J., & Sack, M. N. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0402-y · Cited by 67 · see citing works
Maldonado, M., Chen, J., Duan, H., Huang, T., Jiang, G., & Zhong, Y. (2021) · Translational Medicine of Aging · doi:10.1016/j.tma.2021.02.001 · Cited by 11 · see citing works
Muñoz López, M., López-Gil, J. F., Ramírez de la piscina Viúdez, X., Baz-Valle, E., & Tornero Aguilera, J. F. (2026) · Cells · doi:10.3390/cells15111041 · Cited by 1 · see citing works
“Among them, SIRT7 has attracted interest because of its prominent nucleolar localization and its involvement in the regulation of Pol I-dependent transcription [183].”
- Authors
- Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., & Guarente, L.
- Affiliations
- Massachusetts Institute of Technology (US)
- German Cancer Research Center (DE)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2006-04-17
- Volume
- 20
- Issue
- 9
- Pages
- 1075-1080
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2171723578
- Cited by
- 629
- References
- 28
- Citations by year
- 2026: 23 · 2025: 22 · 2024: 20 · 2023: 34 · 2022: 25 · 2021: 50 · 2020: 33 · 2019: 28 · 2018: 43 · 2017: 35 · 2016: 37 · 2015: 41 · 2014: 28 · 2013: 54 · 2012: 36
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- SIRT7, sirtuins, RNA polymerase I, rDNA transcription, nucleolus, histone deacetylation, cell proliferation, apoptosis, cell viability
- MeSH terms
- Animals, Cell Line, Cell Survival, DNA, Ribosomal, Histones, Humans, RNA Polymerase I, Transcriptional Activation, Apoptosis, Genes, rRNA, RNA Interference, Sirtuins, Cell Proliferation, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review