Structural and Enzymatic Activity Studies of Arabidopsis Histone Deacetylase 6
Date Issued
2014
Date
2014
Author(s)
Wang, Wen-Jiun
Abstract
In eukaryotes, histone modifications regulate many developmental processes by controlling dynamic changes in chromatin structure for gene expression. Histone acetylation is often correlated with transcriptional activation, whereas histone deacetylation is involved in transcriptional repression. Histone acetylation homeostasis is determined by antagonist actions of histone acetyltransferases and histone deacetylases. The Arabidopsis thaliana histone deacetylase 6 (AtHDA6) has diverse roles to regulate genome stability, development status and environmental stress responses in plants. The molecular structures of the histone deacetylases in Arabidopsis have not been resolved for revealing the regulation in molecular level. In this study, we reported a ~25 nm spherical structure of HDA6 superstructure using transmission electron microscopy. For functional assays, we identified different expression patterns of HDAC activity between the endogenous and recombinant HDA6 proteins. In contrast of barely detectable HDAC activity in recombinant HDA6, the HDA6 extracted from 35S: GFP-HDA6 plants showed obviously HDAC activity. Here we presented the 3D structural reconstruction model of HDA6 superstructure, the resolution was about 15.3 A. Moreover, our data indicated that like class I human HDACs, Arabidopsis HDA6 was regulated by posttranslational modification. We identified for the first time that there were two specific phosphorylation sites (Ser427 and Ser429) in Arabidopsis HDA6. These two phosphorylation residues were specifically conserved in known class I HDACs, suggesting that they might be involved in the specificity for HDAC enzymatic activity.
Subjects
阿拉伯芥
組蛋白去乙醯化酵素
三維結構重組
Type
thesis
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