6J6T

Crystal Structure of HDA15 HD domain

6J6T の概要

• エントリーDOI: 10.2210/pdb6j6t/pdb
• 分子名称: Histone deacetylase 15, ZINC ION, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: histone deacetylase, arabidopsis, gene regulation
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 156677.88

構造登録者

Cheng, Y.S.,Hsu, J.C.,Hung, H.C.,Liu, T.C. (登録日: 2019-01-15, 公開日: 2020-01-22, 最終更新日: 2023-11-22)

主引用文献

Chen, C.Y.,Tu, Y.T.,Hsu, J.C.,Hung, H.C.,Liu, T.C.,Lee, Y.H.,Chou, C.C.,Cheng, Y.S.,Wu, K.
Structure of Arabidopsis HISTONE DEACETYLASE15.
Plant Physiol., 184:1585-1600, 2020

PubMed Abstract: 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 (). 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 Ser-448 and Ser-452 in etiolated seedlings. The HDA15 phosphorylation status determines its subnuclear 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.

PubMed: 32878973
DOI: 10.1104/pp.20.00604

実験手法

X-RAY DIFFRACTION (2.36 Å)