The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Involvement of Arabidopsis HOS15 in histone deacetylation and cold tolerance
Open accessAbstract
Histone modification in chromatin is one of the key control points in gene regulation in eukaryotic cells. Protein complexes composed of histone acetyltransferase or deacetylase, WD40 repeat protein, and many other components have been implicated in this process. Here, we report the identification and functional characterization of HOS15, a WD40-repeat protein crucial for repression of genes associated with abiotic stress tolerance through histone deacetylation in Arabidopsis . HOS15 shares high sequence similarity with human transducin-beta like protein (TBL), a component of a repressor protein complex involved in histone deacetylation. Mutation of the HOS15 gene renders mutant plants hypersensitive to freezing temperatures. HOS15 is localized in the nucleus and specifically interacts with histone H4. The level of acetylated histone H4 is higher in the hos15 mutant than in WT plants. Moreover, the stress inducible RD29A promoter is hyperinduced and associated with a substantially higher level of acetylated histone H4 in the hos15 mutant under cold stress conditions. Our results suggest a critical role for gene activation/repression by histone acetylation/deacetylation in plant acclimation and tolerance to cold stress.
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Cites
Smyth, G. K. (2004) · Statistical Applications in Genetics and Molecular Biology · doi:10.2202/1544-6115.1027 · Cited by 11,829
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
Histone acetylation and transcriptional regulatory mechanisms
Struhl, K. (1998) · Genes & Development · doi:10.1101/gad.12.5.599 · Cited by 1,815 · cited 1×
“Hyperacetylation of histones H2B, H3, and H4 has been generally associated with transcriptionally active chromatin (5), whereas the chromatin of inactive regions is enriched in deacetylated histones (6).”
BackgroundYoon, H., Chan, D. W., Huang, Z., Li, J., Fondell, J. D., Qin, J., & Wong, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg120 · Cited by 444
Ahringer, J. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(00)02066-7 · Cited by 388
Cited by
Research on plant abiotic stress responses in the post‐genome era: past, present and future
Hirayama, T., & Shinozaki, K. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04124.x · Cited by 1,215
Epigenetic regulation of stress responses in plants
Chinnusamy, V., & Zhu, J.-K. (2009) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2008.12.006 · Cited by 1,162
Self-citationPhysiological and molecular changes in plants grown at low temperatures
Theocharis, A., Clément, C., & Barka, E. A. (2012) · Planta · doi:10.1007/s00425-012-1641-y · Cited by 773
Epigenetic regulation in plant abiotic stress responses
Chang, Y., Zhu, C., Jiang, J., Zhang, H., Zhu, J., & Duan, C. (2020) · Journal of Integrative Plant Biology · doi:10.1111/jipb.12901 · Cited by 533
Self-citationThe interaction between OsMADS57 and OsTB1 modulates rice tillering via DWARF14
Guo, S., Xu, Y., Liu, H., Mao, Z., Zhang, C., Ma, Y., Zhang, Q., Meng, Z., & Chong, K. (2013) · Nature Communications · doi:10.1038/ncomms2542 · Cited by 367
Metadata
- Authors
- Zhu, J., Jeong, J. C., Zhu, Y., Sokolchik, I., Miyazaki, S., Zhu, J.-K., Hasegawa, P. M., Bohnert, H. J., Shi, H., Yun, D.-J., & Bressan, R. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-03-25
- Volume
- 105
- Issue
- 12
- Pages
- 4945-4950
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2160061988
- Cited by
- 306
- References
- 5
- FWCI
- 19.28
- Type
- journal article
- Language
- en
- Open access
- green
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- Zhu, J., Jeong, J. C., Zhu, Y., Sokolchik, I., Miyazaki, S., Zhu, J.-K., Hasegawa, P. M., Bohnert, H. J., Shi, H., Yun, D.-J., & Bressan, R. A. (2008). Involvement of Arabidopsis HOS15 in histone deacetylation and cold tolerance. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0801029105
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