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

94 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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