酿酒酵母蛋白酶体盖子亚基Rpn12的主链H、C和N共振归属
Backbone H, C and N resonance assignments of the proteasome lid subunit Rpn12 from Saccharomyces cerevisiae.
作者信息
Niu Xiaogang, Ma Shuaipeng, Hu Yunfei, Jin Changwen
机构信息
College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China.
Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing, 100871, China.
出版信息
Biomol NMR Assign. 2020 Apr;14(1):147-150. doi: 10.1007/s12104-020-09935-w. Epub 2020 Feb 19.
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 H, C and N 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.
26S蛋白酶体在泛素-蛋白酶体系统中降解特定的多聚泛素化蛋白，该系统是真核细胞中程序性蛋白降解的主要途径。酿酒酵母Rpn12定位于26S蛋白酶体中19S调节颗粒的盖子部位，在招募外在泛素受体Rpn10中发挥作用。Rpn12包含一个N端TPR（四三肽重复）样结构域和一个C端WH（翼状螺旋）结构域。已观察到Rpn12与19S的几个亚基相互作用，并且它可能在泛素化底物与蛋白酶体结合后19S调节颗粒重排中发挥重要作用。在此，我们报道了酿酒酵母Rpn12主链H、C和N原子的共振归属，这为使用NMR技术进一步研究Rpn12亚基的动力学和相互作用提供了有价值的信息。
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