1H, 13C and 15N resonance assignments of Rpn9, a regulatory subunit of 26S proteasome from Saccharomyces cerevisiae
- 影响因子：
0.0
- 发表刊物：
Biomol. NMR Assign.
- 摘要：
The 26S proteasome is an essential molecular machine for specific protein degradation in eukaryotic cells. The 26S proteasome is formed by a central 20S core particle capped by two 19S regulatory particle (RP) at both ends. The Rpn9 protein is a non-ATPase subunit located in the lid complex of the 19S RP, and is identified to be essential for efficient assembly of yeast 26S proteasome. Bioinformatics analysis of Saccharomyces cerevisiae Rpn9 suggested it contains a PCI domain at the C-terminal region. However, high-resolution structures of either the PCI domain or the full-length Rpn9 still remain elusive. Herein, we report the chemical shift assignments of (1)H, (13)C and (15)N atoms of the individual N- and C-domains, as well as full-length S. cerevisiae Rpn9, which provide the basis for further structural and functional studies of Rpn9 using solution NMR technique.
- 论文类型：
期刊论文
- 论文编号：
41
- 卷号：
8
- 期号：
2
- 页面范围：
307-311
- 是否译文：
否
- 发表时间：
2014-10-08
- 收录刊物：
SCI
- 第一作者：
Wu Yujie
- 通讯作者：
Jin Changwen
- 全部作者：
Hu Yunfei
