The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Targeted Recruitment of the Sin3-Rpd3 Histone Deacetylase Complex Generates a Highly Localized Domain of Repressed Chromatin In Vivo
Open accessAbstract
Eukaryotic organisms contain a multiprotein complex that includes Rpd3 histone deacetylase and the Sin3 corepressor. The Sin3-Rpd3 complex is recruited to promoters by specific DNA-binding proteins, whereupon it represses transcription. By directly analyzing the chromatin structure of a repressed promoter in yeast cells, we demonstrate that transcriptional repression is associated with localized histone deacetylation. Specifically, we observe decreased acetylation of histones H3 and H4 (preferentially lysines 5 and 12) that depends on the DNA-binding repressor (Ume6), Sin3, and Rpd3. Mapping experiments indicate that the domain of histone deacetylation is highly localized, occurring over a range of one to two nucleosomes. Taken together with previous observations, these results define a novel mechanism of transcriptional repression which involves targeted recruitment of a histone-modifying activity and localized perturbation of chromatin structure.
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Citations
Cites
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
Histone acetylation and transcriptional regulatory mechanisms
Struhl, K. (1998) · Genes & Development · doi:10.1101/gad.12.5.599 · Cited by 1,815
Self-citationNuclear Receptor Repression Mediated by a Complex Containing SMRT, mSin3A, and Histone Deacetylase
Nagy, L., Kao, H.-Y., Chakravarti, D., Lin, R. J., Hassig, C. A., Ayer, D. E., Schreiber, S. L., & Evans, R. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80218-4 · Cited by 1,230
Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex
Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (1997) · Cell · doi:10.1016/s0092-8674(00)80216-0 · Cited by 578
Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo
Kadosh, D., & Struhl, K. (1998) · Genes & Development · doi:10.1101/gad.12.6.797 · Cited by 234
Self-citation
Cited by
Zhang, Y., Ng, H.-H., Erdjument-Bromage, H., Tempst, P., Bird, A., & Reinberg, D. (1999) · Genes & Development · doi:10.1101/gad.13.15.1924 · Cited by 1,103
Molecular networks regulating Arabidopsis seed maturation, after‐ripening, dormancy and germination
Holdsworth, M. J., Bentsink, L., & Soppe, W. J. J. (2008) · New Phytologist · doi:10.1111/j.1469-8137.2008.02437.x · Cited by 964
Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00429-4 · Cited by 754
Histone acetylation and deacetylation in yeast
Kurdistani, S. K., & Grunstein, M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1075 · Cited by 677
Single-Nucleosome Mapping of Histone Modifications in S. cerevisiae
Liu, C. L., Kaplan, T., Kim, M., Buratowski, S., Schreiber, S. L., Friedman, N., & Rando, O. J. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030328 · Cited by 499
Metadata
- Authors
- Kadosh, D., & Struhl, K.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1998-09-01
- Volume
- 18
- Issue
- 9
- Pages
- 5121-5127
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W1867241955
- Cited by
- 320
- References
- 5
- FWCI
- 11.48
- Type
- journal article
- Language
- en
- Open access
- green
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