Backbone 1H, 13C and 15N resonance assignments of the proteasome lid subunit Rpn12 from Saccharomyces cerevisiae.
- 影响因子：
0.0
- DOI码：
10.1007/s12104-020-09935-w
- 发表刊物：
Biomol NMR Assign
- 关键字：
Proteasome; Regulatory particle; Rpn12.
- 摘要：
The 26S proteasome degrades selected polyubiquitinated proteins in the ubiquitin-proteasome system, which is the major pathway for programmed protein degradation in eukaryotic cells. The Saccharomyces cerevisiae Rpn12 locates in the lid of the 19S regulatory particle within the 26S proteasome and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. Rpn12 contains a N-terminal TPR (tetratrico peptide repeat)-like domain and a C-terminal WH (winged helix) domain. Interaction of Rpn12 with several subunits of 19S has been observed and it may play an important role in the 19S regulatory particle rearrangement after ubiquitylated substrate binding to the proteasome. Herein, we report the resonance assignments of backbone 1H, 13C and 15N atoms of the Saccharomyces cerevisiae Rpn12, which provide valuable information for further studies of the dynamics and interactions of the Rpn12 subunit using NMR techniques.
- 论文编号：
64
- 卷号：
14
- 期号：
1
- 页面范围：
147-150
- 是否译文：
否
- 发表时间：
2020-04-14
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Xiaogang Niu
- 通讯作者：
Changwen Jin
- 全部作者：
Shuaipeng Ma,Yunfei Hu
