Repository logo
  • English
  • 中文
Log In
Have you forgotten your password?
  1. Home
  2. College of Life Science / 生命科學院
  3. Plant Biology / 植物科學研究所
  4. Structural and Enzymatic Activity Studies of Arabidopsis Histone Deacetylase 6
 
  • Details

Structural and Enzymatic Activity Studies of Arabidopsis Histone Deacetylase 6

Date Issued
2014
Date
2014
Author(s)
Wang, Wen-Jiun
URI
http://ntur.lib.ntu.edu.tw//handle/246246/262832
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
File(s)
Loading...
Thumbnail Image
Name

ntu-103-R01b42022-1.pdf

Size

23.32 KB

Format

Adobe PDF

Checksum

(MD5):c56b4358be39cfd55f6b34e8d87e5b1b

臺大位居世界頂尖大學之列,為永久珍藏及向國際展現本校豐碩的研究成果及學術能量,圖書館整合機構典藏(NTUR)與學術庫(AH)不同功能平台,成為臺大學術典藏NTU scholars。期能整合研究能量、促進交流合作、保存學術產出、推廣研究成果。

To permanently archive and promote researcher profiles and scholarly works, Library integrates the services of “NTU Repository” with “Academic Hub” to form NTU Scholars.

總館學科館員 (Main Library)
醫學圖書館學科館員 (Medical Library)
社會科學院辜振甫紀念圖書館學科館員 (Social Sciences Library)

開放取用是從使用者角度提升資訊取用性的社會運動,應用在學術研究上是透過將研究著作公開供使用者自由取閱,以促進學術傳播及因應期刊訂購費用逐年攀升。同時可加速研究發展、提升研究影響力,NTU Scholars即為本校的開放取用典藏(OA Archive)平台。(點選深入了解OA)

  • 請確認所上傳的全文是原創的內容,若該文件包含部分內容的版權非匯入者所有,或由第三方贊助與合作完成,請確認該版權所有者及第三方同意提供此授權。
    Please represent that the submission is your original work, and that you have the right to grant the rights to upload.
  • 若欲上傳已出版的全文電子檔,可使用Open policy finder網站查詢,以確認出版單位之版權政策。
    Please use Open policy finder to find a summary of permissions that are normally given as part of each publisher's copyright transfer agreement.
  • 網站簡介 (Quickstart Guide)
  • 使用手冊 (Instruction Manual)
  • 線上預約服務 (Booking Service)
  • 方案一:臺灣大學計算機中心帳號登入
    (With C&INC Email Account)
  • 方案二:ORCID帳號登入 (With ORCID)
  • 方案一:定期更新ORCID者,以ID匯入 (Search for identifier (ORCID))
  • 方案二:自行建檔 (Default mode Submission)
  • 方案三:學科館員協助匯入 (Email worklist to subject librarians)

Built with DSpace-CRIS software - Extension maintained and optimized by 4Science