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The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription
Open accessAbstract
Mammalian chromatin remodeling complexes are involved in both activation and repression of transcription. Here, we show that NoRC, a SNF2h- containing nucleolar chromatin remodeling complex, represses ribosomal gene transcription. NoRC-mediated rDNA silencing was alleviated by trichostatin A, indicating that histone deacetylation is causally involved in silencing. Chromatin immunoprecipitation experiments demonstrate that overexpression of TIP5, the large subunit of NoRC, mediates deacetylation of nucleosomes in the vicinity of the rDNA promoter. Protein-protein interaction assays reveal association of TIP5 with the histone deacetylase HDAC1 in vivo and in vitro. Deletion of the C-terminal PHD finger and bromodomain abolishes the interaction of TIP5 and HDAC1, and abrogates transcriptional repression. The results suggest that NoRC silences the rDNA locus by targeting the SIN3 corepressor complex to the rDNA promoter, thereby establishing a repressed chromatin structure.
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“Silent rRNA genes in mammalian cells are known to have hypermethylated DNA and regular nucleosomes carrying repressive histone modifications, such as H3K9me3, H4K20me3 and H3K27me3 (94,95,102,103)”
From Impaired function of rDNA transcription initiation machinery leads to derepression of ribosomal genes with insertions of R2 retrotransposon (2022) · cites this paper as [102]
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Cites
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Histone acetylation and transcriptional regulatory mechanisms
Struhl, K. (1998) · Genes & Development · doi:10.1101/gad.12.5.599 · Cited by 1,815
Ikaros DNA-Binding Proteins Direct Formation of Chromatin Remodeling Complexes in Lymphocytes
Kim, J., Sif, S., Jones, B., Jackson, A., Koipally, J., Heller, E., Winandy, S., Viel, A., Sawyer, A., Ikeda, T., et al. (1999) · Immunity · doi:10.1016/s1074-7613(00)80034-5 · Cited by 587
Santoro, R., Li, J., & Grummt, I. (2002) · Nature Genetics · doi:10.1038/ng1010 · Cited by 406
Self-citationAhringer, J. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(00)02066-7 · Cited by 388
Histone deacetylases: transcriptional repression with SINers and NuRDs
Ayer, D. E. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01536-6 · Cited by 274
p53 represses ribosomal gene transcription
Budde, A., & Grummt, I. (1999) · Oncogene · doi:10.1038/sj.onc.1202402 · Cited by 157
Self-citation
Flagged first, then by citations
Research works printed but not linked: 39
- Bozhenok L, Wade PA and Varga‐Weisz P (2002) WSTF–ISWI chromatin remodeling complex targets heterochromatic replication foci. EMBO J, 21, 2231–2241. · DOI · Paper page
- Brehm A, Nielsen SJ, Miska EA, McCance DJ, Reid JL, Bannister AJ and Kouzarides T (1999) The E7 oncoprotein associates with Mi2 and histone deacetylase activity to promote cell growth. EMBO J, 18, 2449–2458. · DOI
- Brown CJ and Robinson WP (2000) The causes and consequences of random and non‐random X chromosome inactivation in humans. Clin Genet, 58, 353–363. · DOI
- Conconi A, Widmer RM, Koller T and Sogo JM (1989) Two different chromatin structures coexit in ribosomal RNA genes throughout the cell cycle. Cell, 57, 753–761. · DOI · Paper page
- Deuring R et al. (2000) The ISWI chromatin‐remodeling protein is required for gene expression and the maintenance of higher order chromatin structure in vivo. Mol Cell, 5, 355–365. · DOI
- Fazzio TG, Kooperberg C, Goldmark JP, Neal C, Basom R, Delrow J and Tsukiyama T (2001) Widespread collaboration of Isw2 and SIN3–Rpd3 chromatin remodeling complexes in transcriptional repression. Mol Cell Biol, 21, 6450–6460. · DOI
- Goldmark JP, Fazzio TG, Estep PW, Church GM and Tsukiyama T (2000) The Isw2 chromatin remodeling complex represses early meiotic genes upon recruitment by Ume6p. Cell, 103, 423–433. · DOI
- Grunstein M (1997) Histone acetylation in chromatin structure and transcription. Nature, 389, 349–352. · DOI · Paper page
- Hirschler‐Laszkiewicz I, Cavanaugh A, Hu Q, Catania J, Avantaggiati ML and Rothblum LI (2001) The role of acetylation in rDNA transcription. Nucleic Acids Res, 29, 4114–4124. · DOI
- Ito T, Tyler JK, Bulger M, Kobayashi R and Kadonaga JT (1996) ATP‐facilitated chromatin assembly with a nucleoplasmin‐like protein from Drosophila melanogaster. J Biol Chem, 271, 25041–25048. · DOI
- Jenuwein J and Allis CD (2001) Translating the histone code. Science, 293, 1074–1080. · DOI · Paper page
- Kingston RE and Narlikar GJ (1999) ATP‐dependent remodeling and acetylation as regulators of chromatin fluidity. Genes Dev, 13, 2339–2352. · DOI
- Knoepfler PS and Eisenman RN (1999) Sin meets NuRD and other tails of repression. Cell, 99, 447–450. · DOI
- Kuzmichev A and Reinberg D (2001) Role of histone deacetylase complexes in the regulation of chromatin metabolism. Curr Top Microbiol Immunol, 254, 35–58.
- Längst G, Blank TA, Becker PB and Grummt I (1997) RNA polymerase I transcription on nucleosomal templates: the transcription termination factor TTF‐I induces chromatin remodeling and relieves transcription. EMBO J, 16, 760–768. · DOI
- Längst G, Becker PB and Grummt I (1998) TTF‐I determines the chromatin architecture of active rDNA promoter. EMBO J, 17, 3135–3145. · DOI
- LeDouarin B et al. (1995) The N‐terminal part of TIF1, a putative mediator of the ligand‐dependent activation function (AF‐2) of nuclear receptor, is fused to B‐raf in the oncogenic protein. EMBO J, 14, 2020–2033. · DOI · Paper page
- LeRoy G, Orphanides G, Lane WS and Reinberg D (1998) Requirement of RSF and FACT for transcription of chromatin templates in vitro. Science, 282, 1900–1904. · DOI
- Miska EA, Karlsson C, Langley E, Nielsen J and Kouzarides T (1999) HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J, 18, 5099–5107. · DOI
- Mizuguchi G, Tsukiyama T, Wisniewski J and Wu C (1997) Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin. Mol Cell, 1, 141–150. · DOI
- Mizzen CA and Allis CD (1998) Linking histone acetylation to transcriptional regulation. Cell Mol Life Sci, 54, 6–20. · DOI
- Muth V, Nadaud S, Grummt I and Voit R (2001) Acetylation of TAFI68, a subunit of TIF‐IB/SL1, activates RNA polymerase I transcription. EMBO J, 20, 1353–1362. · DOI
- Mutskov VJ, Russanova VR, Dimitrov SI and Pashev IG (1996) Histones associated with nonnucleosomal rat ribosomal genes are acetylated while those bound to nucleosome‐organized gene copies are not. J Biol Chem, 271, 11852–11857. · DOI
- Ng HH and Bird A (2000) Histone deacetylases: silencers for hire. Trends Biochem Sci, 25, 121–126. · DOI
- Pazin MJ and Kadonaga JT (1997) What's up and down with histone deacetylation and transcription? Cell, 89, 325–328. · DOI
- Roth SY, Denu JM and Allis CD (2001) Histone acetyltransferases. Annu Rev Biochem, 70, 81–120. · DOI
- Santoro R and Grummt I (2001) Molecular mechanisms mediating methylation dependent silencing of ribosomal gene transcription. Mol Cell, 8, 719–725. · DOI
- Santoro R, Li J and Grummt I (2002) The nucleolar remodeling complex NoRC silences ribosomal gene transcription. Nat Genet, in press.
- Schnapp A and Grummt I (1996) Purification, assay, and properties of RNA polymerase I and class I‐specific transcription factors in mouse. Methods Enzymol, 273, 233–248. · DOI
- Schultz DC, Friedman JR and Rauscher FJ,III (2001) Targeting histone deacetylase complexes via KRAB‐zinc finger proteins: the PHD and bromodomains of KAP‐1 form a cooperative unit that recruits a novel isoform of the Mi‐2α subunit of NuRD. Genes Dev, 15, 428–443. · DOI
- Sterner DE and Berger SL (2000) Acetylation of histones and transcription‐related factors. Microbiol Mol Biol Rev, 64, 435–459. · DOI
- Strahl BD and Allis CD (2000) The language of covalent histone modifications. Nature, 403, 41–45. · DOI · Paper page
- Strohner R, Nemeth A, Jansa P, Hoffmann‐Rohrer U, Santoro R, Längst G and Grummt I (2001) NoRC—a novel member of mammalian ISWI‐containing chromatin remodeling machines. EMBO J, 20, 4892–4900. · DOI
- Turner BM (2000) Histone acetylation and an epigenetic code. BioEssays, 22, 836–845. · DOI
- Tyler JK and Kadonaga JT (1999) The ‘dark side’ of chromatin remodeling: repressive effects on transcription. Cell, 99, 443–446. · DOI
- Varga‐Weisz P (2001) ATP‐dependent chromatin remodeling factors: nucleosome shufflers with many missions. Oncogene, 20, 3076–3085. · DOI
- Venturini L et al. (1999) TIF1γ, a novel member of the transcriptional intermediary factor 1 family. Oncogene, 18, 1209–1217. · DOI
- Voit R, Hoffmann M and Grummt I (1999) Phosphorylation by G1‐specific cdk–cyclin complexes activates the nucleolar transcription factor UBF. EMBO J, 18, 1891–1899. · DOI
- Zhang Y, LeRoy G, Seelig HP, Lane WS and Reinberg D (1998) The dermatomyositis‐specific autoantigen Mi‐2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell, 95, 279–289. · DOI
Cited by
Sorted by citations
Items 101–200 of 213
Leone, S., Bär, D., Slabber, C. F., Dalcher, D., & Santoro, R. (2017) · EMBO Reports · doi:10.15252/embr.201744330 · Cited by 52
“In somatic mouse and human cells, establishment of heterochromatin at rRNA genes is mediated by TIP5 through its association with the long non-coding (lnc)RNA pRNA, DNA methyl-transferases, and histone modifier enzymes [3,15 – 17].”
Self-citationPutative involvement of the histone acetyltransferase Tip60 in ribosomal gene transcription
Halkidou, K. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh296 · Cited by 51
“its HAT activity; (iii) Tip60 may modulate ribosomal transcription through its direct interaction with HDAC1, an established repressor of ribosomal transcription (8,83).”
BackgroundHemleben, V., Volkov, R. A., Zentgraf, U., & Medina, F. J. (2004) · Progress in botany · doi:10.1007/978-3-642-18819-0_5 · Cited by 47
Disruption of spatiotemporal hypoxic signaling causes congenital heart disease in mice
Yuan, X., Qi, H., Li, X., Wu, F., Fang, J. C., Bober, E., Dobreva, G. D., Zhou, Y., & Braun, T. W. (2017) · Journal of Clinical Investigation · doi:10.1172/jci88725 · Cited by 43
Self-citationCanonical and Noncanonical Actions of Arabidopsis Histone Deacetylases in Ribosomal RNA Processing
Chen, X., Lü, L., Qian, S., Scalf, M., Smith, L. M., & Zhong, X. (2018) · The Plant Cell · doi:10.1105/tpc.17.00626 · Cited by 54
“In mammals, HDAC1 is recruited to specific rDNA loci by Nucleolar Remodeling Complex (NoRC) or transcription factor RUNX2 and represses rDNA transcription (Zhou et al., 2002; Ali et al., 2012).”
BackgroundProteomic Characterization of the Nucleolar Linker Histone H1 Interaction Network
Szerlong, H. J., Herman, J., Krause, C., DeLuca, J. G., Skoultchi, A. I., Winger, Q. A., Prenni, J. E., & Hansen, J. C. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.01.001 · Cited by 46
“The observed disagreement between the immunoblot and SpC analyses of HDAC1 levels is likely attributable to the detection of identical peptides derived from alternative HDAC1 isoforms or HDAC family members by LC-MS/MS, while amino acids 467-482 were exclusively detected by the αHDAC1 antibody used in the immunoblot a…”
BackgroundInfluentialTargeting chromatin remodelers: Signals and search mechanisms
Erdel, F., Krug, J., Längst, G., & Rippe, K. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.06.005 · Cited by 44
“The NoRC complex, composed of Snf2H and TIP5, acts as a repressor of rRNA transcription [55,104].”
BackgroundDNA methylation‐mediated nucleosome dynamics and oncogenic Ras signaling
Patra, S. K., & Szyf, M. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06658.x · Cited by 39
Human SMARCA5 is continuously required to maintain nucleosome spacing
Bomber, M. L., Wang, J., Liu, Q., Barnett, K. R., Layden, H. M., Hodges, E. C., Stengel, K. R., & Hiebert, S. W. (2023) · Molecular Cell · doi:10.1016/j.molcel.2022.12.018 · Cited by 58
MicroRNA 100: a context dependent miRNA in prostate cancer
Leite, K., Morais, D. R., Reis, S., Viana, N., Moura, C., Flórez, M., Silva, I., Dip, N., & Srougi, M. (2013) · Clinics · doi:10.6061/clinics/2013(06)12 · Cited by 44
A Runx2-HDAC1 co-repressor complex regulates rRNA gene expression by modulating UBF acetylation
Ali, S. A., Dobson, J. R., Lian, J. B., Stein, J. L., van Wijnen, A. J., Zaidi, S. K., & Stein, G. S. (2012) · Journal of Cell Science · doi:10.1242/jcs.100909 · Cited by 41
“NoRC also recruits HDAC1 to rRNA genes (Zhou et al., 2002).”
BackgroundLi, Y., Ge, C., & Franceschi, R. (2009) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.090705 · Cited by 44
BEND3 represses rDNA transcription by stabilizing a NoRC component via USP21 deubiquitinase
Khan, A. A., Giri, S., Wang, Y., Chakraborty, A., Ghosh, A. K., Anantharaman, A., Aggarwal, V., Sathyan, K. M., Ha, T., Prasanth, K. V., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1424705112 · Cited by 48
“NoRC targets histone-modifying enzymes and DNA methyltransferase to rDNA to establish a heterochromatic state that inhibits transcription activation (7, 9, 10).”
BackgroundCECR2 Is Involved in Spermatogenesis and Forms a Complex with SNF2H in the Testis
Thompson, P. J., Norton, K. A., Niri, F., Dawe, C. E., & McDermid, H. E. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.11.041 · Cited by 36
An intranucleolar body associated with rDNA
Hutten, S., Prescott, A. R., James, J. L., Riesenberg, S., Boulon, S., Lam, Y. W., & Lamond, A. I. (2011) · Chromosoma · doi:10.1007/s00412-011-0327-8 · Cited by 34
“The mammalian nucleolar remodelling complex is responsible for the coordination of factors regulating heterochromatin formation on rDNA (Santoro and Grummt 2005; Santoro et al. 2002; Strohner et al. 2001; Zhou et al. 2002).”
BackgroundHisaoka, M., Ueshima, S., Murano, K., Nagata, K., & Okuwaki, M. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00299-10 · Cited by 36
“recruits the Sin3 corepressor complex (27, 42).”
ISWI chromatin remodeling in ovarian somatic and germ cells: revenge of the NURFs.
Pépin, D., Vanderhyden, B., Picketts, D., & Murphy, B. (2007) · Trends in endocrinology and metabolism · doi:10.1016/j.tem.2007.05.004 · Cited by 39
Burgio, G., Rocca, G. L., Sala, A., Arancio, W., Gesù, D. D., Collesano, M., Sperling, A., Armstrong, J. A., van Heeringen, S. V., Logie, C., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000089 · Cited by 38
“The mammalian ISWI homolog, SNF2H, is part of the nucleolar remodeler NoRC complex, that has been shown to be involved in the repression of Pol I-dependent transcription [17,18].”
BackgroundNucleosome Remodeler SNF2L Suppresses Cell Proliferation and Migration and Attenuates Wnt Signaling
Eckey, M., Kuphal, S., Straub, T., Rümmele, P., Kremmer, E., Bosserhoff, A., & Becker, P. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06619-11 · Cited by 36
“Many studies focused on SNF2H, which is considered the major ISWI-type remodeler in the cell, as it is ubiquitously expressed and is part of abundant chromatin-remodeling complexes that are functionally diverse, ranging from chromatin assembly to rDNA transcriptional repression (7, 55).”
BackgroundBreaking new ground: Digging into TERRA function
Maicher, A., Lockhart, A., & Luke, B. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.012 · Cited by 37
Brown, E., Malakar, S., & Krebs, J. E. (2007) · Biochemistry and Cell Biology · doi:10.1139/o07-059 · Cited by 27
Manelytė, L., Strohner, R., Gross, T. J., & Längst, G. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004157 · Cited by 35
Xie, T., He, Y., Korkeamäki, H., Zhang, Y., Imhoff-Manuel, R. D., Lohi, O., & Radhakrishnan, I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.252494 · Cited by 36
Vanolst, L., Fromental-Ramain, C., & Ramain, P. (2005) · Development · doi:10.1242/dev.02014 · Cited by 29
“Recent studies have also shown that a mouse Iswi-containing complex, NoRC, plays an essential role during repression of transcription of the rDNA locus by RNA polymerase I (Strohner et al., 2001; Santoro et al., 2002; Zhou et al., 2002).”
BackgroundMoehren, U. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh621 · Cited by 32
Matzinger, M., Schmücker, A., Yelagandula, R., Stejskal, K., Krššáková, G., Berger, F., Mechtler, K., & Mayer, R. (2024) · Nature Communications · doi:10.1038/s41467-024-45391-z · Cited by 30
Anosova, I., Melnik, S., Tripsianes, K., Kateb, F., Grummt, I., & Sattler, M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv365 · Cited by 32
“The C-terminal part of TIP5 harbors a tandem PHD finger/bromodomain, a cooperative unit that interacts with chromatin modifying enzymes, which set specific heterochromatic histone marks and trigger de novo DNA methylation (3,4).”
BackgroundSelf-citationLarge-scale organization of ribosomal DNA chromatin is regulated by Tip5
Zillner, K., Filarsky, M., Rachow, K., Weinberger, M., Längst, G., & Németh, A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt218 · Cited by 30
“The role of Tip5 in the inactivation of rRNA transcription has been demonstrated to involve cooperation with proteins, such as TTF-I, HDACs and Dnmts (12,14,17).”
BackgroundEpigeneitc silencing of ribosomal RNA genes by Mybbp1a
Tan, B. C., Yang, C., Hsieh, C.-L., Chou, Y.-H., Zhong, C. Z., Yung, B. Y., & Liu, H. (2012) · Journal of Biomedical Science · doi:10.1186/1423-0127-19-57 · Cited by 36
“Given the requirement of HDACs in maintaining an inactive state of rDNA promoters [26,30], and the reported association of Mybbp1a with several HDACs-containing co-repressor complexes [10], we next aimed to assess whether HDACs contribute to Mybbp1a-mediated rDNA gene silencing.”
BackgroundEpigenetic Engineering of Ribosomal RNA Genes Enhances Protein Production
Santoro, R., Lienemann, P. S., & Fussenegger, M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006653 · Cited by 28
Self-citationLessard, F., Stefanovsky, V. Y., Tremblay, M. G., & Moss, T. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks198 · Cited by 27
“However, recruitment of this same chromatin remodelling complex along with the deacetylase HDAC1 and a DNA methyltransferase has also been shown to repress the rRNA genes (19,20).”
BackgroundFeng, S., & Manley, J. (2022) · Genes & Development · doi:10.1101/gad.349969.122 · Cited by 28
“For example, pRNAs recruit the chromatin remodeling complex NoRC, which targets HDAC1, to the rDNA promoter region and further represses Pol I transcription in response to stress (Fig. 2; Zhou et al. 2002; Mayer et al. 2008).”
BackgroundMorais, D. R., Reis, S., Viana, N., Piantino, C., Massoco, C., Moura, C., Dip, N., Silva, I., Srougi, M., & Leite, K. (2014) · Cancer Cell International · doi:10.1186/s12935-014-0119-3 · Cited by 28
Liu, Y., Mattila, J., Ventelä, S., Yadav, L., Zhang, W., Lamichane, N., Sundström, J. T. T., Kauko, O., Grenman, R. A., Varjosalo, M. T., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.09.022 · Cited by 33
“This regulation occurs through epigenetic changes (McStay and Grummt, 2008); acetylation of histone H4 and tri-methylation of histone H3 lysine 4 correlates with a transcriptionally active rRNA gene, whereas methylation of histone H3 lysine 9 corresponds to a silent rRNA gene (Santoro and Grummt, 2005; Wang et al., 20…”
BackgroundAnalysis of histone modifications at human ribosomal DNA in liver cancer cell
Yu, F., Shen, X., Li, F., & Yu, Z. (2015) · Scientific Reports · doi:10.1038/srep18100 · Cited by 32
Shen, M., Zhou, T., Xie, W., Ling, T., Zhu, Q., Zong, L., Lyu, G., Gao, Q., Zhang, F., & Tao, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062668 · Cited by 20
“These factors affect transcription by recruitment of enzymes that modify histone methylation and acetylation [5,15,29].”
BackgroundChromatin Remodeling Factors and DNA Replication
Varga‐Weisz, P. (2005) · Springer eBooks · doi:10.1007/3-540-27310-7_1 · Cited by 23
Non-Coding RNA-Driven Regulation of rRNA Biogenesis
Kaliatsi, E. G., Γιαρίμογλου, Ν., Stathopoulos, C., & Stamatopoulou, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249738 · Cited by 28
“The recruitment of NoRC to rDNA promotes H3K9me3 histone methylations and removal of H4ac acetylation marks but also causes a nucleosome shift that blocks RNA pol I access to the rDNA promoter [31].”
BackgroundEmelyanov, A., Vershilova, E., Ignatyeva, M., Pokrovsky, D., Lu, X., Konev, A., & Fyodorov, D. (2012) · Genes & Development · doi:10.1101/gad.180604.111 · Cited by 26
“MammalianNoRC can also regulate replication of rDNA in cultured cells (Zhou et al. 2002; Li et al. 2004) throughmechanisms that involve histone and DNAmethylation (Santoro and Grummt 2005) and IGS transcripts (Mayer et al.”
BackgroundNakagawa, T., Hattori, S., Nobuta, R., Kimura, R., Nakagawa, M., Matsumoto, M., Nagasawa, Y., Funayama, R., Miyakawa, T., Inada, T., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101030 · Cited by 27
Shi, G. W., Wu, M., Fang, L., Yu, F., Cheng, S., Li, J., Du, J. X., & Wong, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.571653 · Cited by 25
“On the other hand, knockdown of PHF2 had no effect on the association of TIP5 (10), the large subunit of NoRC complex, with the rDNA promoter (Fig.”
BackgroundMermoud, J. E., Rowbotham, S. P., & Varga‐Weisz, P. (2011) · Cell Cycle · doi:10.4161/cc.10.23.18558 · Cited by 35
Banks, C. A. S., Thornton, J. L., Kempf, C. G., Adams, M. K., Miah, S., Boanca, G., Liu, X., Katt, M. L., Parmely, T. J., Florens, L. A., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir118.000661 · Cited by 29
“For example, the TIP5 subunit of the chromatin remodeling complex NoRC, which targets HDAC1 containing complexes to ribosomal gene promoters (52), binds to pRNA, promoting a more open configuration exposing new interaction surfaces (53).”
BackgroundTsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y., & Cristea, I. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015156 · Cited by 36
Treacle Sticks the Nucleolar Responses to DNA Damage Together
Gál, Z., Nieto, B., Boukoura, S., Rasmussen, A. V., & Larsen, D. H. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.892006 · Cited by 25
Quantitative analysis of NOR expression in a B chromosome of the grasshopper Eyprepocnemis plorans
Teruel, M., Cabrero, J., Perfectti, F., & Camacho, J. P. M. (2008) · Chromosoma · doi:10.1007/s00412-008-0197-x · Cited by 18
“It works by recruiting DNA-methylating and histone-modifying activities to the rDNA promoter, thus determining a repressive higher-order chromatin structure (Santoro et al. 2002; Zhou et al. 2002 ).”
BackgroundNoRC Recruitment by H2A.X Deposition at rRNA Gene Promoter Limits Embryonic Stem Cell Proliferation
Eleuteri, B., Aranda, S., & Ernfors, P. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.023 · Cited by 27
Nucleolar Reorganization Upon Site-Specific Double-Strand Break Induction
Franek, M., Kovaříková, A. S., Bártová, E., & Kozubek, S. (2016) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155416668505 · Cited by 26
He, Y., Imhoff-Manuel, R. D., Sahu, A., & Radhakrishnan, I. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp051 · Cited by 19
“SAP30 has previously been shown to direct the Sin3 corepressor complex to the nucleolus (49) and its DNA-binding activity might have a similar role in directing the complex to the promoter regions of ribosomal DNA, a well-known target for Sin3/HDAC-mediated gene repression (50,51).”
BackgroundThe Role of rDNA Clusters in Global Epigenetic Gene Regulation
Tchurikov, N. A., & Kravatsky, Y. V. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.730633 · Cited by 23
“Silent rDNA units are characterized by DNA methylation in their promoter regions and by the presence of repressive histone marks, such as H3K9me2, H3K9me3, and deacetylated histones (Zhou et al., 2002).”
BackgroundING1 regulates rRNA levels by altering nucleolar chromatin structure and mTOR localization
Rajarajacholan, U. K., Thalappilly, S., & Riabowol, K. T. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1161 · Cited by 23
“Chromatin regulators like HDAC1 (14), DNMT1 (13), SMARCAD1 (15), PARP1 (16), SIRT1 and SUV39H1 (17) are mediators of NoRC-mediated transcriptional silencing of rDNA.”
BackgroundBEND3 mediates transcriptional repression and heterochromatin organization
Khan, A. A., & Prasanth, S. G. (2015) · Transcription · doi:10.1080/21541264.2015.1100228 · Cited by 20
“The role of NoRC in rDNA silencing is well documented.(9,10,22) Overexpression of BEND3 phenocopies most of the Tip5 gain-of-function phenotypes observed with regard to epigenetic changes at the rDNA locus.”
BackgroundHuang, S., Rothblum, L. I., & Chen, D. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-089 · Cited by 19
Many players, one goal: how chromatin states are inherited during cell division
Santoro, R., & Lucia, F. D. (2005) · Biochemistry and Cell Biology · doi:10.1139/o05-021 · Cited by 17
“, DNA methylation, hypoacetylation of histone H4, dimethylation of lysine 9 of histone H3, and nucleosome remodeling (Santoro et al. 2002; Zhou et al. 2002; Santoro and Grummt 2005).”
BackgroundSelf-citationEukaryotic Methyl-CpG-Binding Domain Proteins and Chromatin Modification
Hung, M., & Shen, C. ‐. J. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.5.841-846.2003 · Cited by 20
“In Drosophila melanogaster, an MBD protein, dMBD2/3, has been characterized that shares significant homology with the vertebrate MBD2 and MBD3 (30, 39).”
BackgroundInfluentialRepression of interrupted and intact rDNA by the SUMO pathway in drosophila melanogaster
Luo, Y., Fefelova, E., Ninova, M., Chen, Y.-C. A., & Aravin, A. A. (2020) · eLife · doi:10.7554/elife.52416 · Cited by 19
“In mammals repression of rDNA units was shown to correlate with the presence of CpG DNA methylation and repressive histone marks near the rDNA promoter (Bird et al., 1981; Coffman et al., 2005; Conconi et al., 1989; Dammann et al., 1993; Flavell et al., 1988; Earley et al., 2006; Li et al., 2006; Santoro and Grummt, 2…”
BackgroundGraveline, R., Marcinkiewicz, K. M., Choi, S., Paquet, M., Wurst, W., Floß, T., & David, G. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00522-16 · Cited by 14
“Experiments in mammalian cells suggest that NoRC, a 411 SNF2h-containing NucleOlar chromatin Remodelling Complex, silences the rDNA locus by 412 targeting the Sin3 corepressor complex to rDNA promoters (49).”
BackgroundSalomon‐Kent, R., Marom, R., John, S., Dundr, M., Schiltz, L., Gutiérrez, J. L., Workman, J. L., Benayahu, D., & Hager, G. L. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.24960 · Cited by 21
“In mammalian cells, chromatin remodeling enzymes have been implicated in both silencing (NoRC) and activation (B-WICH) of ribosomal genes (Santoro et al., 2002; Zhou et al., 2002; Percipalle and Farrants, 2006).”
BackgroundStępiński, D. (2012) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2012.09.001 · Cited by 20
Zhai, N., Zhao, Z.-L., Cheng, M.-B., Di, Y., Yan, H., Cao, C.-Y., Dai, H., Zhang, Y., & Shen, Y. (2012) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjs003 · Cited by 19
“However, our data indicate that TTF-I interacts only with TIP5, a subunit of the silencing NoRC complex (Strohner et al., 2001; Zhou et al., 2002).”
BackgroundConstitutive Expression of Short Hairpin RNA in Vivo Triggers Buildup of Mature Hairpin Molecules
Ahn, M., Witting, S. R., Ruiz, R., Saxena, R., & Morral, N. (2011) · Human Gene Therapy · doi:10.1089/hum.2010.234 · Cited by 14
“…arrest); endosomal vesicle formation; intracellular protein transport; chromatin-remodeling genes (such as Baz2a, a gene shown to inhibit ribosomal RNA [rRNA] synthesis; Zhou et al. , 2002); ubiquitination; gene silencing; helicase activity (Table 3; the full gene list is available on request).”
Mayer, R., Matzinger, M., Schmücker, A., Stejskal, K., Krššáková, G., Berger, F., & Mechtler, K. (2022) · bioRxiv · doi:10.1101/2022.09.01.506203 · Cited by 16
The Epigenetics of the Nucleolus: Structure and Function of Active and Silent Ribosomal RNA Genes
Santoro, R. (2011) · Springer eBooks · doi:10.1007/978-1-4614-0514-6_4 · Cited by 13
“3) modified either with active and/or with a specific set of silent marks (H3K9me2) (Prior et al. 1983; Schwartz and Ahmad 2005; Yuan et al. 2007; Zhou et al. 2002).”
BackgroundSelf-citationFefelova, E. A., Pleshakova, I. M., Mikhaleva, E. A., Pirogov, S. A., Poltorachenko, V. A., Abramov, Y. A., Romashin, D. D., Shatskikh, A. S., Blokh, R. S., Gvozdev, V. A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1276 · Cited by 15
“Silent rRNA genes in mammalian cells are known to have hypermethylated DNA and regular nucleosomes carrying repressive histone modifications, such as H3K9me3, H4K20me3 and H3K27me3 (94,95,102,103) (see (26–29) for reviews).”
BackgroundInfluentialLing, T., Xie, W., Luo, M., Shen, M., Zhu, Q., Zong, L., Zhou, T., Gu, J., Lu, Z., Zhang, F., et al. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.06.045 · Cited by 16
Neben, C. L., Tuzon, C. T., Mao, X., Lay, F. D., & Merrill, A. E. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx209 · Cited by 20
“Silencing of rDNA is mediated by the nucleolar-remodeling complex (NoRC), which recruits HDACs and DNA methyltransferases to establish the structural characteristics of heterochromatin (36,37).”
BackgroundLalioti, V. S., Vergarajauregui, S., Villasanté, A., Pulido, D., & Sandoval, I. V. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24355 · Cited by 16
“…complex (NoRC) interactswith the SIN3 co-repressor complex, which contains the histone deacetylases HDAC1 and HDAC2 (Santoro et al., 2002; Zhou et al., 2002; McStay and Grummt, 2008) to modulate DNAmethylation and histone acetylation and structure, thereby controlling…”
BackgroundPreuss, S. B., Costa‐Nunes, P., Tucker, S., Pontes, O., Lawrence, R. J., Mosher, R. A., Kasschau, K. D., Carrington, J. C., Baulcombe, D. C., Viegas, W. S., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.009 · Cited by 155
Changes in gene expression in response to altered SHL transcript levels
Müssig, C., & Altmann, T. (2003) · Plant Molecular Biology · doi:10.1023/b:plan.0000023661.65248.4b · Cited by 14
“Zhou et al. (2002) provided another example.”
BackgroundInfluentialPlata, M. P., Kang, H. J., Zhang, S., Kuruganti, S., Hsu, S.-J., & Labrador, M. (2009) · Chromosoma · doi:10.1007/s00412-008-0198-9 · Cited by 12
“Heterochromatin protein 1 and dimethylated histone H3 at lysine 9 partially correlate with condensed DAPI-stained nucleolar rDNA In addition to deacetylation of H3, heterochromatin formation in rDNA is also accompanied by deacetylation of histone H4 (Earley et al. 2006; Zhou et al. 2002).”
BackgroundInfluentialUniting the paths to gene silencing
Pikaard, C. S., & Lawrence, R. J. (2002) · Nature Genetics · doi:10.1038/ng1008 · Cited by 12
Epigenetics of Ribosomal RNA Genes
Denisenko, O. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922140097 · Cited by 10
“1 2022 lase), further promoting transcriptional repressive state [21, 23, 27].”
BackgroundAgarwal, D., Kumari, R., Ilyas, A., Tyagi, S., Kumar, R., & Poddar, N. K. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.10.026 · Cited by 12
Regulatory roles of nucleolus organizer region-derived long non-coding RNAs
Hao, Q., & Prasanth, K. V. (2021) · Mammalian Genome · doi:10.1007/s00335-021-09906-z · Cited by 11
Liu, M., Guo, A.-L., Boukhgalter, B., Heuvel, K. V. D., Tripp, M., & Pape, L. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf683 · Cited by 10
“Furthermore, a nucleolar, chromatin remodeling activity that associates with the RNA pol I termination factor, TTF-I, was characterized in mammals (46), which aids in repressing rRNA synthesis by targeting histone deacetylase (47).”
BackgroundPlatt, J. L., Kent, N. A., Kimmel, A. R., & Harwood, A. J. (2017) · Genome Research · doi:10.1101/gr.216309.116 · Cited by 8
“…with distinct genetic elements and genomic regions, interact with epigenetic regulators, and act with different functions to activate or repress gene regulation (Zhou et al. 2002; Srinivasan et al. 2008; Yang and Seto 2008; Dorighi and Tamkun 2013; Wu et al. 2014; de Dieuleveult et al. 2016).”
The role of ATP-dependent chromatin remodeling complexes in regulation of genetic processes
Mazina, M., & Vorobyeva, N. (2016) · Russian Journal of Genetics · doi:10.1134/s1022795416050082 · Cited by 9
“Another example of the involvement of the complexes of the ISWI family in transcription repres sion is the hNoRC complex, which was first described as a repressor of transcription of rRNA genes by RNA polymerase I [58, 59].”
BackgroundFuentes, E. N., Zuloaga, R., Nardocci, G., de la Reguera, C. F., Simonet, N. G., Fumeron, R., Valdés, J. A., Molina, A., & Álvarez, M. (2014) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2014.04.005 · Cited by 10
“This leads to the deacetylation and methylation of Histone 3 Lysine 9 (H3K9) and to CpG DNA methylation at the rDNA promoter, all of which silences rDNA transcription (Santoro et al., 2002; Zhou et al., 2002; Li et al., 2006).”
BackgroundMeraner, J., Lechner, M., Schwarze, F., Gander, R., Jesacher, F., & Loidl, P. (2008) · Cell Biology International · doi:10.1016/j.cellbi.2008.04.018 · Cited by 7
“In mammalian cells the chromatin remodeling complex NoRC silences the rDNA locus by targeting HDAC1 to the ribosomal gene promoter (Zhou et al., 2002); the interaction of the PHD finger as well as the bromodomain of NoRC components is necessary for rDNA silencing, and the acetylation state of…”
BackgroundThe human SIN3B corepressor forms a nucleolar complex with leukemia-associated ETO homologues
Dhanda, R. S., Lindberg, S. R., & Olsson, I. (2008) · BMC Molecular Biology · doi:10.1186/1471-2199-9-8 · Cited by 8
“Furthermore, involvement of the SIN3 corepressor complex in rDNA silencing has been reported [43].”
BackgroundChapter 6 Chromatin Remodeling and Nuclear Receptor Signaling
Buranapramest, M., & Chakravarti, D. (2009) · Progress in molecular biology and translational science · doi:10.1016/s1877-1173(09)87006-3 · Cited by 11
“In addition, both domains are required for recruitingHDACs andDNMTs to rDNA promoters.(202) Therefore, TIP5 functions to (1) position nucleosomes by directing Snf2hATPase activity and (2) recruit repressive histonemodifying enzymes to the promoter.”
BackgroundBiochemistry of Multiprotein HDAC Complexes
Vaquero, A., Scher, M. B., & Reinberg, D. (2006) · Humana Press eBooks · doi:10.1385/1-59745-024-3:23 · Cited by 7
“NoRC, an SNF2h-containing nucleolar chromatin remodeling complex that represses ribosomal gene transcription, has also been shown to recruit Sin3 (40).”
BackgroundBreindl, M., Spitzer, D., Gerasimaitė, R., Kairys, V., Schubert, T. E. O., Henfling, R., Schwartz, U., Lukinavičius, G., & Manelytė, L. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1096 · Cited by 9
“Baz2A forms a NoRC chromatin remodeling complex with Snf2H, repositioning nucleosomes at ribosomal DNA ( rDNA ) promoter regions and acting as a chromatin-specific repressor of rDNA transcription by recruiting histone modifying and DNA methylating activities ( 36 ,37 ) .”
BackgroundMercury chloride alters heterochromatin domain organization and nucleolar activity in mouse liver
Zannino, L., Pagano, A., Casali, C., Oldani, M., Balestrazzi, A., & Biggiogera, M. (2022) · Histochemistry and Cell Biology · doi:10.1007/s00418-022-02151-8 · Cited by 6
“Baz2a is an essential component of the NoRC (nucleolar remodeling complex), a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (Zhou et al. 2002).”
BackgroundTogether we are on together we are off -a conserved rule for ribosomal RNA (rRNA) gene regulation?
Saradadevi, G. P., Priyadarshini, N., Bera, A., & Mohannath, G. (2020) · Journal of Plant Biochemistry and Biotechnology · doi:10.1007/s13562-020-00610-8 · Cited by 4
Rolicka, A. T., Guo, Y., Zapater, A. G., Tariq, K., Quin, J. E., Vintermist, A., Sadeghifar, F., Arsenian‐Henriksson, M., & Farrants, A. Ö. (2020) · The FASEB Journal · doi:10.1096/fj.202000411r · Cited by 9
Hainer, S. J., & Martens, J. A. (2011) · Transcription · doi:10.4161/trns.2.3.15684 · Cited by 6
“23,24 In mammals, the silencing of ribosomal DNA (rDNA) by heterochromatin formation is mediated by small ncRNAs that are transcribed from rDNA promoter regions.”
Cai, Y., & Laughon, A. (2009) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagrm.2009.01.001 · Cited by 6
ISWI chromatin remodeling complexes recruit NSD2 and H3K36me2 in pericentromeric heterochromatin
Gotō, N., Suke, K., Yonezawa, N., Nishihara, H., Handa, T., Sato, Y., Kujirai, T., Kurumizaka, H., Yamagata, K., & Kimurâ, H. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202310084 · Cited by 9
“NoRC suppresses rRNA transcription by inducing DNA methylation and histone deacetylation on the ribosomal DNA (rDNA) promoter in the nucleolus (Zhou et al., 2002; Santoro et al., 2002).”
Epigenetic Programming of the rRNA Promoter by MBD3
Brown, S. E., & Szyf, M. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01880-06 · Cited by 73
“It has been previously reported through chromatin immunoprecipitation assays, however, that HDAC1 does bind to the rRNA promoter (54); therefore, a complete lack of these proteins in the nucleolus is unlikely.”
BackgroundChromatin Organization and the Mammalian Nucleolus
Németh, A., & Längst, G. (2013) · Springer eBooks · doi:10.1007/978-94-007-5818-6_6 · Cited by 4
Multi-omics analysis of thermogenic lipolysis in brown adipocytes
Mattanovich, M., Anagho, H. A., Argemi‐Muntadas, L., Nielsen, M. L., Gao, Q., & Möritz, T. (2025) · iScience · doi:10.1016/j.isci.2025.113382 · Cited by 5
“Hells, involved in DNA methylation and Smarca5, involved in DNA replication, and in the recruitment of DNA methyltransferases for rDNA silencing 73 also contribute.”
DNA damage repair and transcription
El‐Osta, A. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4173-1 · Cited by 4
Lyu, G., Zong, L., Zhang, C., Huang, X., Xie, W., Fang, J., Guan, Y., Zhang, L., Ni, T., Gu, J., et al. (2018) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjy023 · Cited by 3
ISWI Chromatin Remodeling Complexes
Tsukiyama, T., Bogenschutz, N. L., Kwong, T. J., Rodríguez, J., Unnikrishnan, A., & Yadon, A. N. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00283-7
Functional Analysis of ISWI Complexes in Mammalian Cells
Bozhenok, L., Poot, R. A., Collins, N., & Varga‐Weisz, P. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)77024-4 · Cited by 3
Deciphering the Role of the Non-Coding Genome in Regulating Gene-Diet Interactions
Law, P. P., & Holland, M. L. (2018) · Nutrients · doi:10.3390/nu10121831 · Cited by 3
“62 However, only a fraction of the rDNA copies within a cell are actively transcribed due to epigenetic 63 regulation [18-22].”
BackgroundMikogai, A., Yanagisawa, J., Yasuzawa-Tanaka, K., & Murayama, A. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.011 · Cited by 2
Chromatin Remodeling in Heart Failure
Han, P., Yang, J., Shang, C., & Chang, C.-P. (2016) · Cardiac and vascular biology · doi:10.1007/978-3-319-41457-7_5 · Cited by 2
Pessoa, J., & Carvalho, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158411 · Cited by 1
“Nucleoli exhibit DNA–RNA segregation as a consequence of several partial gene silencing mechanisms, including DNA methylation [30], histone modifications [31], chromatin remodeling [32,33], and interactions with intergenic RNAs [34].”
Background
Metadata
- Authors
- Zhou, Y., Santoro, R., & Grummt, I.
- Affiliations
- German Cancer Research Center (DE)
- Corresponding author
- Grummt, Ingrid
- Venue
- The EMBO Journal
- Published
- 2002-09-02
- Volume
- 21
- Issue
- 17
- Pages
- 4632-4640
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC126197
- OpenAlex
- W2045365624
- Cited by
- 234
- References
- 0
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 6 · 2023: 4 · 2022: 9 · 2021: 5 · 2020: 8 · 2019: 6 · 2018: 11 · 2017: 6 · 2016: 12 · 2015: 9 · 2014: 10 · 2013: 12 · 2012: 15
- FWCI
- 4.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsches Krebsforschungszentrum
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- norC, HDAC1, histone deacetylation, ribosomal DNA transcription, rDNA silencing, RNA polymerase I, PHD finger, bromodomain, transcriptional repression
- MeSH terms
- Bromodomain Containing Proteins, Acetylation, Animals, Cell Line, Chromatin, Chromosomal Proteins, Non-Histone, DNA, Ribosomal, Histone Deacetylases, Histones, Multienzyme Complexes, Nucleosomes, Promoter Regions, Genetic, Protein Processing, Post-Translational, Recombinant Fusion Proteins, RNA Polymerase I, Transcription, Genetic, Trans-Activators, 3T3 Cells, Protein Structure, Tertiary, Genes, rRNA, Amino Acid Motifs, Gene Silencing, Protein Interaction Mapping, Macromolecular Substances, Mice, Sin3 Histone Deacetylase and Corepressor Complex, Histone Deacetylase 1
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