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The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity

  • Chung ke Chang
  • , Tzong Huah Wu
  • , Chu Ya Wu
  • , Ming hui Chiang
  • , Elsie Khai Woon Toh
  • , Yin Chih Hsu
  • , Ku Feng Lin
  • , Yu heng Liao
  • , Tai huang Huang*
  • , Joseph Jen Tse Huang
  • *此作品的通信作者

研究成果: 雜誌貢獻期刊論文同行評審

115   連結會在新分頁中開啟 引文 斯高帕斯(Scopus)

摘要

TDP-43 is a DNA/RNA-binding protein associated with different neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-U). Here, the structural and physical properties of the N-terminus on TDP-43 have been carefully characterized through a combination of nuclear magnetic resonance (NMR), circular dichroism (CD) and fluorescence anisotropy studies. We demonstrate for the first time the importance of the N-terminus in promoting TDP-43 oligomerization and enhancing its DNA-binding affinity. An unidentified structural domain in the N-terminus is also disclosed. Our findings provide insights into the N-terminal domain function of TDP-43.

原文英語
頁(從 - 到)219-224
頁數6
期刊Biochemical and Biophysical Research Communications
425
發行號2
DOIs
出版狀態已發佈 - 2012 8月 24

ASJC Scopus subject areas

  • 生物物理學
  • 生物化學
  • 分子生物學
  • 細胞生物學

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