The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity - PubMed (original) (raw)

. 2012 Aug 24;425(2):219-24.

doi: 10.1016/j.bbrc.2012.07.071. Epub 2012 Jul 23.

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

Chung-ke Chang et al. Biochem Biophys Res Commun. 2012.

Abstract

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.

Copyright © 2012 Elsevier Inc. All rights reserved.

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