NMR 1 H, 13 C, 15 N backbone and side chain resonance assignment of the N-terminal domain of yeast proteasome lid subunit Rpn5

The 26S proteasome is responsible for the selective, ATP-dependent degradation of polyubiquitinated proteins in eukaryotic cells. It consists of a 20S barrel-shaped core particle capped by two 19S regulatory particle at both ends. The Rpn5 subunit is a non-ATPase subunit located in the lid subcomplex of the 19S regulatory particle and is identified to inhibit the Rpn11 deubiquitinase activity in the isolated lid. The protein contains a C-terminal proteasome–CSN–eIF3 (PCI) domain and an N-terminal α-solenoid domain, the latter has been shown to be highly flexible in the isolated lid and may participate in interactions with different subunits of the proteasome. We herein report the 1 H, 13 C and 15 N atoms chemical shift assignments of the N-terminal domain (residues 1–136) of Saccharomyces cerevisiae Rpn5, which provide the basis for further studies of the structure, dynamics and interactions of the Rpn5 subunit by NMR technique.