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Arabidopsis thaliana histone deacetylase1(AtHD1)is localized in euchromatic regions and demonstrates histone deacetylase activity in vitro 被引量:6

Arabidopsis thaliana histone deacetylase1(AtHD1)is localized in euchromatic regions and demonstrates histone deacetylase activity in vitro
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摘要 Arabidopsis thaliana histone deacetylase 1 (AtHD1 or AtHDA19), a homolog ot yeast RPD3, is a global regulator ot many physiological and developmental processes in plants. In spite of the genetic evidence for a role of AtHD1 in plant gene regulation and development, the biochemical and cellular properties ofAtHD 1 are poorly understood. Here we report cellular localization patterns ofAtHD 1 in vivo and histone deacetylase activity in vitro. The transient and stable expression of a green fluorescent protein (GFP)-tagged AtHD1 in onion cells and in roots, seeds and leaves of the transgenic Arabidopsis, respectively, revealed that AtHD1 is localized in the nucleus presumably in the euchromatic regions and excluded from the nucleolus. The localization patterns ofAtHD 1 are different from those of AtHD2 and AtHDA6 that are involved in nucleolus formation and silencing of transgenes and repeated DNA elements, respectively. In addition, a histone deacetylase activity assay showed that the recombinant AtHD 1 produced in bacteria demonstrated a specific histone deacetylase activity in vitro. The data suggest that AtHD 1 is a nuclear protein and possesses histone deacetylase activities responsible for global transcriptional regulation important to plant growth and development.
出处 《Cell Research》 SCIE CAS CSCD 2006年第5期479-488,共10页 细胞研究(英文版)
基金 We thank Mary Bryk and Timothy Hall for critical suggestions to improve the manuscript,David Stelly and Keerti Rathore for assistance in GFP localization studies in onion cells,and Stanislav Vitha in the Microscopy and Imaging Center at Texas A&M University for technical support for epifluorescence microscopic image analysis in the transgenic plants.The work is supported by grants from the National Institutes of Health(GM067015) the National Science Foundation Plant Genome Research Program(DBI0077774)to Z J C.
关键词 ARABIDOPSIS histone deacetylase RPD3 subcellular localization gene silencing CHROMATIN 组蛋白脱乙酰基1 常染色体 基因抑制 植物
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  • 1Binder A, Bohm L. Influence of irradiation and pentoxifylline on histone H3 phosphorylation in human tumour cell lines. Cell Prolif 2002; 35:37-47. 被引量:1
  • 2Koshlaud D, Strunnikov A. Mitotic chromosome condensation.Annu Rev Cell Dev Biol. 1996; 12:305-33. 被引量:1
  • 3Yang Q, Chen JT, Geng ZH, Yu XD, Huang XT. Studies of distribution of phosphorylated H3 in human MCF-7 cells by immunofluroescence labeling. Acta Genetica Sinica 2002; 29:471-5 (Article in Chinese). 被引量:1
  • 4Goto H, Tomono Y, Ajiro K, et al. Identification of a noval phosphorylation site on histone H3 coupled with mitotic chromosome condensation. J Biol Chem 1999; 274:25543-9. 被引量:1
  • 5Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000; 403:41-5. 被引量:1
  • 6Van Hooser A, Goodrich DW, Allis CD, Brinkley BR, ManciniMA. Histone H3 phosphorylation is required for the initiation,but not maintenance, of mammalian chromosome condensation.J Cell Sci 1998; 111:3497-506. 被引量:1
  • 7de La Barre AE, Gerson V, Gout S, et al. Core histone N-termini play an essential role in mitotic chromosome condensation. EMBO J 2000; 19:379-91. 被引量:1
  • 8Hsu JY, Sun ZW, Li X, et al. Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 2000; 102:279-91. 被引量:1
  • 9Speliotes EK, Uren A, Vaux D, Horvitz HR. The survivin-like C.elegans BIR-1 protein acts with the Aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone. Mol Cell 2000; 6:211-23. 被引量:1
  • 10Roth S, Allis CD. Chromatin condensation: does histone H1dephosphorylation play a role? Trends Biol Sci 1992; 17:93-8. 被引量:1

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