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A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Abstract
Trapoxin is a microbially derived cyclotetrapeptide that inhibits histone deacetylation in vivo and causes mammalian cells to arrest in the cell cycle. A trapoxin affinity matrix was used to isolate two nuclear proteins that copurified with histone deacetylase activity. Both proteins were identified by peptide microsequencing, and a complementary DNA encoding the histone deacetylase catalytic subunit (HD1) was cloned from a human Jurkat T cell library. As the predicted protein is very similar to the yeast transcriptional regulator Rpd3p, these results support a role for histone deacetylase as a key regulator of eukaryotic transcription.
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“This is consistent with the fact that both genes encode proteins involved in histone modification and chromatin remodeling [21,23-25,30-33].”
From A genome-wide screen for modifiers of transgene variegation identifies genes with critical roles in development (2008) · cites this paper as [31]
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Cites
Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
Clipstone, N. A., & Crabtree, G. R. (1992) · Nature · doi:10.1038/357695a0 · Cited by 1,635
The ancient regulatory-protein family of WD-repeat proteins
Neer, E. J., Schmidt, C. J., Nambudripad, R., & Smith, T. F. (1994) · Nature · doi:10.1038/371297a0 · Cited by 1,491
A positive role for histone acetylation in transcription factor access to nucleosomal DNA
Lee, D. Y., Hayes, J. J., Pruss, D., & Wolffe, A. P. (1993) · Cell · doi:10.1016/0092-8674(93)90051-q · Cited by 1,122
Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.Preprint
Braunstein, M., Rose, A. B., Holmes, S. G., Allis, C. D., & Broach, J. R. (1993) · Genes & Development · doi:10.1101/gad.7.4.592 · Cited by 791
Hecht, A., Laroche, T., Strahl‐Bolsinger, S., Gasser, S. M., & Grunstein, M. R. (1995) · Cell · doi:10.1016/0092-8674(95)90512-x · Cited by 780
Yoshida, M., Horinouchi, S., & Beppu, T. (1995) · BioEssays · doi:10.1002/bies.950170510 · Cited by 715
Aparicio, O. M., Billington, B. L., & Gottschling, D. E. (1991) · Cell · doi:10.1016/0092-8674(91)90049-5 · Cited by 697
Kijima, M., Yoshida, M., Sugita, K., Horinouchi, S., & Beppu, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41547-5 · Cited by 516
Identification of a Gene Encoding a Yeast Histone H4 Acetyltransferase
Kleff, S., Andrulis, E. D., Anderson, C. W., & Sternglanz, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.42.24674 · Cited by 353
Genetic Analysis of Histone H4: Essential Role of Lysines Subject to Reversible Acetylation
Megee, P. C., Morgan, B. A., Mittman, B. A., & Smith, M. M. (1990) · Science · doi:10.1126/science.2106160 · Cited by 349
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Kester, H. A., Blanchetot, C., den Hertog, J., van der Saag, P. T., & van der Burg, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27439 · Cited by 118
Ashe, A., Morgan, D. K., Whitelaw, N. C., Bruxner, T. J., Vickaryous, N. K., Cox, L. L., Butterfield, N. C., Wicking, C., Blewitt, M. E., Wilkins, S. J., et al. (2008) · Genome Biology · doi:10.1186/gb-2008-9-12-r182 · Cited by 117
Jung, J., Park, J.-H., Lee, S., To, T. K., Kim, J.-M., Seki, M., & Park, C. (2013) · The Plant Cell · doi:10.1105/tpc.113.118364 · Cited by 117
Histone H2A.Z Acetylation Modulates an Essential Charge Patch
Ren, Q., & Gorovsky, M. A. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00269-6 · Cited by 117
Histone deacetylases as therapeutic targets in hematologic malignancies
Melnick, A. M., & Licht, J. D. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200207000-00010 · Cited by 117
Tagami, T., Park, Y., & Jameson, J. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22345 · Cited by 121
Tian, L., Wang, J., Fong, M. P., Chen, M., Cao, H., Gelvin, S. B., & Chen, Z. J. (2003) · Genetics · doi:10.1093/genetics/165.1.399 · Cited by 116
Trichostatin and Leptomycin: Inhibition of Histone Deacetylation and Signal‐Dependent Nuclear Export
Yoshida, M., & Horinouchi, S. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb09397.x · Cited by 118
In vitro assays for the determination of histone deacetylase activity
Heltweg, B., Trapp, J., & Jung, M. (2005) · Methods · doi:10.1016/j.ymeth.2005.03.003 · Cited by 116
Chemical genetics: exploring and controlling cellular processes with chemical probes
Crews, C. M., & Splittgerber, U. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01425-5 · Cited by 116
Identification of Mouse Histone Deacetylase 1 as a Growth Factor-Inducible Gene
Bartl, S., Taplick, J., Egger, G., Khier, H., Kuchler, K., & Seiser, C. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.9.5033 · Cited by 115
Expression and Function of Histone Deacetylases in Rheumatoid Arthritis Synovial Fibroblasts
Horiuchi, M., Morinobu, A., Chin, T., Sakai, Y., Kurosaka, M., & Kumagai, S. (2009) · The Journal of Rheumatology · doi:10.3899/jrheum.081115 · Cited by 114
Proteome-wide prediction of acetylation substrates
Basu, A. B., Rose, K. L., Zhang, J., Beavis, R. C., Ueberheide, B. M., Garcia, B. A., Chait, B. T., Zhao, Y., Hunt, D. F., Segal, E., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906801106 · Cited by 115
Structural Biasing Elements for In-Cell Histone Deacetylase Paralog Selectivity
Wong, J. C., Hong, R., & Schreiber, S. L. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0341440 · Cited by 114
Self-citationHistone deacetylase 3 associates with and represses the transcription factor GATA-2
Ozawa, Y., Towatari, M., Tsuzuki, S., Hayakawa, F., Maeda, T., Miyata, Y., Tanimoto, M., & Saito, H. (2001) · Blood · doi:10.1182/blood.v98.7.2116 · Cited by 115
Alland, L., David, G., Shen-Li, H., Potes, J., Muhle, R., Lee, H.-C., Hou, H., Chen, K., & DePinho, R. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.8.2743-2750.2002 · Cited by 113
Application of omics- and multi-omics-based techniques for natural product target discovery
Zhang, H., Lv, C., Zhang, L., Guo, X., Shen, Y., Nagle, D. G., Zhou, Y., Liu, S., Zhang, W., & Luan, X. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111833 · Cited by 115
Yang, W., Yao, Y., & Seto, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4814 · Cited by 112
Kurtev, V., Margueron, R., Kroboth, K., Ogris, E., Cavaillès, V., & Seiser, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312300200 · Cited by 112
Zhang, Y., & Dufau, M. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204417200 · Cited by 112
Solari, F., Bateman, A. G., & Ahringer, J. (1999) · Development · doi:10.1242/dev.126.11.2483 · Cited by 112
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Kunadis, E., Lakiotaki, E., Korkolopoulou, P. A., & Piperi, C. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107721 · Cited by 113
Han, Z., Yu, H., Zhao, Z., Hunter, D., Luo, X., Duan, J., & Tian, L. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00310 · Cited by 110
Suzuki, T., Nagano, Y., Kouketsu, A., Matsuura, A., Maruyama, S., Kurotaki, M., Nakagawa, H., & Miyata, N. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049207j · Cited by 110
ER stress response plays an important role in aggregation of α-synuclein
Jiang, P., Gan, M., Ebrahim, A. S., Lin, W.-L., Melrose, H. L., & Yen, S.-H. C. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-56 · Cited by 110
Recent Advances in Chemical Approaches to the Study of Biological Systems
Shogren‐Knaak, M. A., Alaimo, P. J., & Shokat, K. M. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.405 · Cited by 111
Sun, Z., & Hampsey, M. (1999) · Genetics · doi:10.1093/genetics/152.3.921 · Cited by 110
Yao, Y.-L., & Yang, W.-M. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2011/146493 · Cited by 120
Sensing of Ionizing Radiation-induced DNA Damage by ATM through Interaction with Histone Deacetylase
Kim, G. D., Choi, Y. H., Dimtchev, A., Jeong, S. J., Dritschilo, A., & Jung, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31127 · Cited by 109
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Codd, R., Braich, N., Liu, J., Soe, C. Z., & Pakchung, A. A. H. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.05.026 · Cited by 109
Berger, S. L. (2001) · Oncogene · doi:10.1038/sj.onc.1204324 · Cited by 108
Deltour, S., Guérardel, C., & Leprince, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14831 · Cited by 108
Dangond, F., Hafler, D. A., Tong, J. K., Randall, J., Kojima, R., Utku, N., & Gullans, S. R. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.8033 · Cited by 108
Homo-oligomerisation and nuclear localisation of mouse histone deacetylase 111Edited by J. Karn
Taplick, J., Kurtev, V., Kroboth, K., Posch, M., Lechner, T., & Seiser, C. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4569 · Cited by 108
Chen, Y.-J. C., Koutelou, E., & Dent, S. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.12.004 · Cited by 110
Functional analysis of a RPD3 histone deacetylase homologue in Arabidopsis thaliana
Wu, K., Malik, K., Tian, L., Brown, D. C., & Miki, B. L. A. (2000) · Plant Molecular Biology · doi:10.1023/a:1006498413543 · Cited by 107
HDAC11 is a regulator of diverse immune functions
Yanginlar, C., & Logie, C. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.12.002 · Cited by 112
Calvo, D., Victor, M., Gay, F., Sui, G., Luke, M. P.-S., Dufourcq, P., Wen, G., Maduro, M., Rothman, J. H., & Shi, Y. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.7197 · Cited by 106
Kim, D., & Lassar, A. B. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8704-8717.2003 · Cited by 106
Philpott, A., Krude, T., & Laskey, R. A. (2000) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.1999.0346 · Cited by 106
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Self-citationBowers, A. A., West, N. H., Newkirk, T. L., Troutman-Youngman, A. E., Schreiber, S. L., Wiest, O., Bradner, J. E., & Williams, R. M. (2009) · Organic Letters · doi:10.1021/ol900078k · Cited by 104
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Inks, E. S., Josey, B. J., Jesinkey, S. R., & Chou, C. J. (2011) · ACS Chemical Biology · doi:10.1021/cb200134p · Cited by 105
Chemoproteomic approaches to drug target identification and drug profiling
Bantscheff, M., & Drewes, G. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.11.003 · Cited by 106
Shim, J. S., Lee, J., Park, H., Park, S. J., & Kwon, H. J. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.08.015 · Cited by 103
Histone acetylation and the cell-cycle in cancer
Wang, C. (2001) · Frontiers in bioscience · doi:10.2741/1wang1 · Cited by 103
Sundqvist, A., Sollerbrant, K., & Svensson, C. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00588-2 · Cited by 103
Effects of histone acetylation and DNA methylation on p21WAF1regulation
Fang, J. (2002) · World Journal of Gastroenterology · doi:10.3748/wjg.v8.i3.400 · Cited by 102
A non-isotopic assay for histone deacetylase activity
Hoffmann, K., Jung, M., Brosch, G., & Loidl, P. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.9.2057 · Cited by 102
Nakao, Y., Yoshida, S., Matsunaga, S., Shindoh, N., Terada, Y., Nagai, K., Yamashita, J. K., Ganesan, A., van Soest, R. W. M., & Fusetani, N. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200602047 · Cited by 102
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Yoshida, M., Kudo, N., Kosono, S., & Ito, A. (2017) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.93.019 · Cited by 109
TEL contacts multiple co-repressors and specifically associates with histone deacetylase-3
Wang, L., & Hiebert, S. W. (2001) · Oncogene · doi:10.1038/sj.onc.1204479 · Cited by 101
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Wells, C. E., Bhaskara, S., Stengel, K. R., Zhao, Y., Sirbu, B. M., Chagot, B., Cortez, D., Khabele, D., Chazin, W., Cooper, A. C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068915 · Cited by 102
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Sommer, A., Hilfenhaus, S., Menkel, A. R., Kremmer, E., Seiser, C., Loidl, P., & Lüscher, B. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00183-7 · Cited by 102
Haery, L., Thompson, R. C., & Gilmore, T. D. (2015) · Genes & Cancer · doi:10.18632/genesandcancer.65 · Cited by 105
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Chang, K. T., & Min, K. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(02)00003-x · Cited by 99
He, Q., Titov, D. V., Li, J., Tan, M., Ye, Z., Zhao, Y., Romo, D., & Liu, J. O. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201408817 · Cited by 98
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Lechner, T., Carrozza, M. J., Yu, Y., Grant, P. A., Eberharter, A., Vannier, D., Brosch, G., Stillman, D. J., Shore, D., & Workman, J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005730200 · Cited by 97
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Moser, M., Hagelkrüys, A., & Seiser, C. (2013) · Chromosoma · doi:10.1007/s00412-013-0441-x · Cited by 99
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Dangond, F., & Gullans, S. R. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8891 · Cited by 96
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Heltweg, B., Dequiedt, F., Verdin, E. M., & Jung, M. (2003) · Analytical Biochemistry · doi:10.1016/s0003-2697(03)00276-8 · Cited by 95
Zhang, X. M., Wharton, W., Yuan, Z., Tsai, S., Olashaw, N., & Seto, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.12.5106-5118.2004 · Cited by 95
Zika, E., Greer, S. F., Zhu, X.-S., & Ting, J. P. ‐. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.9.3091-3102.2003 · Cited by 94
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Volk, A. G., Liang, K., Suraneni, P. K., Li, X., Zhao, J., Bulic, M., Marshall, S. A., Pulakanti, K., Malinge, S., Taub, J. W., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.10.004 · Cited by 96
Reeves, M. B., Murphy, J., Greaves, R. F., Fairley, J. A., Brehm, A., & Sinclair, J. H. (2006) · Journal of Virology · doi:10.1128/jvi.01297-06 · Cited by 96
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Parthun, M. R. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.07.006 · Cited by 95
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Imai, Y., Kurokawa, M., Yamaguchi, Y., Izutsu, K., Nitta, E., Mitani, K., Satake, M., Noda, T., Ito, Y., & Hirai, H. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.1033-1043.2004 · Cited by 95
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Davie, J. (1997) · Molecular Biology Reports · doi:10.1023/a:1006811817247 · Cited by 92
Sauer, P. V., Gu, Y., Liu, W. H., Mattiroli, F., Panne, D., Luger, K., & Churchill, M. E. A. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky823 · Cited by 91
Analogues of trichosтatin a and trapoxin B as histone deacetylase inhibitors
Jung, M., Hoffmann, K., Brosch, G., & Loidl, P. (1997) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(97)00284-9 · Cited by 91
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Lin, H., Zhao, L., & Cheng, S.-Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203380200 · Cited by 90
Chemical Genetic Modifier Screens
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Self-citationHuang, S., Qiu, Y., Shi, Y., Xu, Z., & Brandt, S. J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.24.6792 · Cited by 91
Comparative analysis of HD2 type histone deacetylases in higher plants
Dangl, M., Brosch, G., Haas, H., Loidl, P., & Lusser, A. (2001) · Planta · doi:10.1007/s004250000506 · Cited by 88
Metadata
- Authors
- Taunton, J., Hassig, C. A., & Schreiber, S. L.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Schreiber, Stuart L.
- Venue
- Science
- Published
- 1996-04-19
- Volume
- 272
- Issue
- 5260
- Pages
- 408-411
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1974112332
- Cited by
- 1,829
- References
- 20
- Citations by year
- 2026: 31 · 2025: 31 · 2024: 33 · 2023: 52 · 2022: 36 · 2021: 48 · 2020: 54 · 2019: 47 · 2018: 64 · 2017: 45 · 2016: 46 · 2015: 56 · 2014: 44 · 2013: 49 · 2012: 61
- FWCI
- 36.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- histone deacetylase, cell cycle arrest, transcriptional regulation, yeast homolog, nuclear proteins, Jurkat cells, protein purification
- MeSH terms
- Amino Acid Sequence, Animals, Anti-Bacterial Agents, Cattle, Cell Cycle, Cloning, Molecular, Enzyme Inhibitors, Fungal Proteins, Gene Expression Regulation, Histone Deacetylases, Humans, Hydroxamic Acids, Molecular Sequence Data, Molecular Weight, Peptides, Saccharomyces cerevisiae, T-Lymphocytes, Transcription Factors, Transcription, Genetic, Tumor Cells, Cultured, Saccharomyces cerevisiae Proteins, Histone Deacetylase Inhibitors
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