Zhu Jianhua, Jeong Jae Cheol, Zhu Yanmei, Sokolchik Irina, Miyazaki Saori, Zhu Jian-Kang, Hasegawa Paul M, Bohnert Hans J, Shi Huazhong, Yun Dae-Jin, Bressan Ray A
State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100094, China.
Proc Natl Acad Sci U S A. 2008 Mar 25;105(12):4945-50. doi: 10.1073/pnas.0801029105. Epub 2008 Mar 20.
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.
染色质中的组蛋白修饰是真核细胞基因调控的关键控制点之一。由组蛋白乙酰转移酶或去乙酰化酶、WD40重复蛋白和许多其他成分组成的蛋白质复合物参与了这一过程。在此,我们报告了HOS15的鉴定和功能表征,HOS15是一种WD40重复蛋白,通过拟南芥中的组蛋白去乙酰化作用对与非生物胁迫耐受性相关的基因的抑制至关重要。HOS15与人类转导素β样蛋白(TBL)具有高度的序列相似性,TBL是参与组蛋白去乙酰化的阻遏蛋白复合物的一个组成部分。HOS15基因突变使突变体植物对冷冻温度高度敏感。HOS15定位于细胞核,并与组蛋白H4特异性相互作用。hos15突变体中乙酰化组蛋白H4的水平高于野生型植物。此外,在冷胁迫条件下,胁迫诱导型RD29A启动子在hos15突变体中被过度诱导,并与显著更高水平的乙酰化组蛋白H4相关。我们的结果表明,组蛋白乙酰化/去乙酰化在植物适应和耐受冷胁迫过程中对基因激活/抑制起着关键作用。