Abstract
Highlights: Black-Right-Pointing-Pointer The N-terminus of TDP-43 contains an independently folded structural domain (NTD). Black-Right-Pointing-Pointer The structural domains of TDP-43 are arranged in a beads-on-a-string fashion. Black-Right-Pointing-Pointer The NTD promotes TDP-43 oligomerization in a concentration-dependent manner. Black-Right-Pointing-Pointer The NTD may assist nucleic acid-binding activity of TDP-43. -- 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.
Chang, Chung-ke;
[1]
Wu, Tzong-Huah;
[2]
Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Institute of Biochemistry, Academia Sinica, Taipei 115, Taiwan (China);
Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan (China)];
Wu, Chu-Ya;
[2]
Graduate Institute of Engineering, National Taiwan University of Science and Technology, Taipei 106, Taiwan (China)];
Chiang, Ming-hui;
Toh, Elsie Khai-Woon;
[1]
Hsu, Yin-Chih;
Lin, Ku-Feng;
[2]
Liao, Yu-heng;
[1]
Huang, Tai-huang;
[1]
Department of Physics, National Taiwan Normal University, Taipei 106, Taiwan (China)];
Huang, Joseph Jen-Tse, E-mail: jthuang@chem.sinica.edu.tw
[2]
- Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan (China)
- Institute of Chemistry, Academia Sinica, Taipei 115, Taiwan (China)
Citation Formats
Chang, Chung-ke, Wu, Tzong-Huah, Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Institute of Biochemistry, Academia Sinica, Taipei 115, Taiwan (China), Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan (China)], Wu, Chu-Ya, Graduate Institute of Engineering, National Taiwan University of Science and Technology, Taipei 106, Taiwan (China)], Chiang, Ming-hui, Toh, Elsie Khai-Woon, Hsu, Yin-Chih, Lin, Ku-Feng, Liao, Yu-heng, Huang, Tai-huang, Department of Physics, National Taiwan Normal University, Taipei 106, Taiwan (China)], and Huang, Joseph Jen-Tse, E-mail: jthuang@chem.sinica.edu.tw.
The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity.
United States: N. p.,
2012.
Web.
doi:10.1016/J.BBRC.2012.07.071.
Chang, Chung-ke, Wu, Tzong-Huah, Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Institute of Biochemistry, Academia Sinica, Taipei 115, Taiwan (China), Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan (China)], Wu, Chu-Ya, Graduate Institute of Engineering, National Taiwan University of Science and Technology, Taipei 106, Taiwan (China)], Chiang, Ming-hui, Toh, Elsie Khai-Woon, Hsu, Yin-Chih, Lin, Ku-Feng, Liao, Yu-heng, Huang, Tai-huang, Department of Physics, National Taiwan Normal University, Taipei 106, Taiwan (China)], & Huang, Joseph Jen-Tse, E-mail: jthuang@chem.sinica.edu.tw.
The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity.
United States.
https://doi.org/10.1016/J.BBRC.2012.07.071
Chang, Chung-ke, Wu, Tzong-Huah, Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Institute of Biochemistry, Academia Sinica, Taipei 115, Taiwan (China), Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan (China)], Wu, Chu-Ya, Graduate Institute of Engineering, National Taiwan University of Science and Technology, Taipei 106, Taiwan (China)], Chiang, Ming-hui, Toh, Elsie Khai-Woon, Hsu, Yin-Chih, Lin, Ku-Feng, Liao, Yu-heng, Huang, Tai-huang, Department of Physics, National Taiwan Normal University, Taipei 106, Taiwan (China)], and Huang, Joseph Jen-Tse, E-mail: jthuang@chem.sinica.edu.tw.
2012.
"The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity."
United States.
https://doi.org/10.1016/J.BBRC.2012.07.071.
@misc{etde_22210200,
title = {The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity}
author = {Chang, Chung-ke, Wu, Tzong-Huah, Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Institute of Biochemistry, Academia Sinica, Taipei 115, Taiwan (China), Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan (China)], Wu, Chu-Ya, Graduate Institute of Engineering, National Taiwan University of Science and Technology, Taipei 106, Taiwan (China)], Chiang, Ming-hui, Toh, Elsie Khai-Woon, Hsu, Yin-Chih, Lin, Ku-Feng, Liao, Yu-heng, Huang, Tai-huang, Department of Physics, National Taiwan Normal University, Taipei 106, Taiwan (China)], and Huang, Joseph Jen-Tse, E-mail: jthuang@chem.sinica.edu.tw}
abstractNote = {Highlights: Black-Right-Pointing-Pointer The N-terminus of TDP-43 contains an independently folded structural domain (NTD). Black-Right-Pointing-Pointer The structural domains of TDP-43 are arranged in a beads-on-a-string fashion. Black-Right-Pointing-Pointer The NTD promotes TDP-43 oligomerization in a concentration-dependent manner. Black-Right-Pointing-Pointer The NTD may assist nucleic acid-binding activity of TDP-43. -- 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.}
doi = {10.1016/J.BBRC.2012.07.071}
journal = []
issue = {2}
volume = {425}
journal type = {AC}
place = {United States}
year = {2012}
month = {Aug}
}
title = {The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity}
author = {Chang, Chung-ke, Wu, Tzong-Huah, Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Institute of Biochemistry, Academia Sinica, Taipei 115, Taiwan (China), Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan (China)], Wu, Chu-Ya, Graduate Institute of Engineering, National Taiwan University of Science and Technology, Taipei 106, Taiwan (China)], Chiang, Ming-hui, Toh, Elsie Khai-Woon, Hsu, Yin-Chih, Lin, Ku-Feng, Liao, Yu-heng, Huang, Tai-huang, Department of Physics, National Taiwan Normal University, Taipei 106, Taiwan (China)], and Huang, Joseph Jen-Tse, E-mail: jthuang@chem.sinica.edu.tw}
abstractNote = {Highlights: Black-Right-Pointing-Pointer The N-terminus of TDP-43 contains an independently folded structural domain (NTD). Black-Right-Pointing-Pointer The structural domains of TDP-43 are arranged in a beads-on-a-string fashion. Black-Right-Pointing-Pointer The NTD promotes TDP-43 oligomerization in a concentration-dependent manner. Black-Right-Pointing-Pointer The NTD may assist nucleic acid-binding activity of TDP-43. -- 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.}
doi = {10.1016/J.BBRC.2012.07.071}
journal = []
issue = {2}
volume = {425}
journal type = {AC}
place = {United States}
year = {2012}
month = {Aug}
}