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 哺乳动物组蛋白去乙酰化酶(HDACs)通过磷酸化来调节其定位、活性和功能。然而，对植物HDAC功能和活性的磷酸化调控知之甚少。
在此，我们报道了拟南芥中还原性钾依赖性3/组蛋白去乙酰化酶1(RPD3/HDA1)Ⅱ型组蛋白去乙酰化酶HDA15的晶体结构。 HDA15HDA15HD的组蛋白去乙酰化酶结构域为四聚体，每个单体由12个α-螺旋和9个β-片层组成。HDA15HD的L1环和β2片层是形成四聚体的重要界面。 
N-末端锌指结构域促进了HDA15HD的二聚化，提高了其酶活性。 此外，在黄化幼苗中，HDA15在Ser448和Ser452处也有磷酸化。HDA15的磷酸化状态决定了其亚核定位和寡聚化。 HDA15的磷酸化部分破坏了它的寡聚化，导致酶活性的丧失和从核仁到核质的移位。 综上所述，这些数据表明磷酸化在调节HDA15的结构和功能中起着关键作用。 Mammalian histone deacetylases (HDACs) undergo phosphorylation to regulate their localization, activity and function. However, little is known about the regulation of plant HDAC function and activity by phosphorylation. Here, we report the crystal structure of the Reduced Potassium Dependency3/Histone Deacetylase1 (RPD3/HDA1) type class II histone deacetylase HDA15 in Arabidopsis (Arabidopsis thaliana). The histone deacetylase domain of HDA15 (HDA15HD) assembles as tetrameric forms with each monomer composed of 12 α-helices and 9 β-sheets. The L1 loop and β2 sheet of HDA15HD are the essential interfaces for the tetramer formation. The N-terminal zinc finger domain enhances HDA15HD dimerization and increases its enzymatic activity. Furthermore, HDA15 can also be phosphorylated at Ser448 and Ser452 in etiolated seedlings. The HDA15 phosphorylation status determines its sub-nuclear localization and oligomerization. Phosphomimetics of HDA15 partially disrupt its oligomerization and cause loss of enzymatic activity and translocation from the nucleolus into nucleoplasm. Together, these data indicate that phosphorylation plays a critical role in regulating the structure and function of HDA15. 版权作品，未经PaperRSS书面授权，严禁转载，违者将被追究法律责任。 PaperRSS，关注生命科学，高校院所科研进展。
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