RPN11 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae.
Murakami Y, Naitou M, Hagiwara H, Shibata T, Ozawa M, Sasanuma S, Sasanuma M, Tsuchiya Y, Soeda E, Yokoyama K
Nature genetics10(3)261-8(1995 Jul)

Report the ubiquitin-bound structure of Rpn11 from S. cerevisiae and the mechanisms for mechanochemical coupling of substrate degradation and deubiquitination.
Title: An AAA Motor-Driven Mechanical Switch in Rpn11 Controls Deubiquitination at the 26S Proteasome.

Overall, this work demonstrates that the co-opted Rpn11p, which is involved in the assembly of the functional proteasome, also functions in the proper assembly of the tombusvirus viral replicase complex.
Title: The proteasomal Rpn11 metalloprotease suppresses tombusvirus RNA recombination and promotes viral replication via facilitating assembly of the viral replicase complex.

Fluorescently labeled tetra-Ub chains revealed endo-chain preference for Ubp6 acting on Lys(48) and random action for Rpn11.
Title: Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6.

A key role for rpn11 in 26S proteasome
Title: Base-CP proteasome can serve as a platform for stepwise lid formation.

The Rpn11 active site at the entrance to the ATPase ring pore is likely to prevent erroneous deubiquitylation of folded proteins.
Title: Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11.