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.

中文翻译：

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酿酒酵母的蛋白酶体盖亚基Rpn12的骨干1H，13C和15N共振分配。

26S蛋白酶体降解遍在蛋白-蛋白酶体系统中的选定的多泛素化蛋白，这是真核细胞中程序化蛋白降解的主要途径。在酿酒酵母Rpn12定位在19S调节颗粒的盖子内26S蛋白酶体起着招募外在泛素受体Rpn10的作用。Rpn12包含一个N端TPR（四肽重复序列）样域和一个C端WH（有翼螺旋）域。已观察到Rpn12与19S的几个亚基的相互作用，并且在泛素化的底物与蛋白酶体结合后，它可能在19S调控颗粒重排中发挥重要作用。在这里，我们报告骨架¹ H，¹³ C和¹⁵的共振分配酿酒酵母Rpn12的N个原子，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。