Tai Kudo

TL;DR: Using mass spectrometry, it is found that Rsp5, a ubiquitin‐ligase in budding yeast, catalyzes the formation of Lys63‐linked Ubiquitin chains in vitro, raising the possibility that Lys63-linked ubiquit in chain also serves as a targeting signal for the 26S proteaseome in vivo.

TL;DR: Four proteasome-interacting proteins (PIPs), Nas2/p27, Nas6/gankyrin, Rpn14/PAAF1, and Hsm3/S5b, bind specific Rpt subunits of the RP and interact each other genetically, suggesting that these proteins are bona fide RP chaperones.

TL;DR: The results suggest that the 26S proteasome completes its assembly process in the cytoplasm and translocates into the nucleus through the nuclear pore complex as a holoenzyme.

TL;DR: It is proposed that free ubiquitin chains function as a Ubiquitin reservoir that allows maintenance of monomeric ubiquitins at adequate levels under normal conditions and rapid supply for substrate conjugation under stress conditions.

TL;DR: The analysis suggests that the assembly of the lid is a highly ordered and multi-step process; first, Rpn5, 6, 8, 9, and 11 are assembled to form a core module, then a second module, consisting of RPN3, 7, and Sem1, is attached, followed by the incorporation of Rpn12 to form the lid complex.