Extended Data Fig. 5: TXNL1 interacts with the catalytic groove of Rpn11, but does not get degraded by the 26S proteasome in isolation, even in the presence of arsenite.
From: Structural landscape of the degrading 26S proteasome reveals conformation-specific binding of TXNL1
a) Arsenite treatment perturbs FAT10 degradation, but does not induce TXNL1 degradation in vitro. Coomassie-stained SDS-PAGE gel showing time points for the degradation of FAT10/NUB1 (5 μM) by the 26S proteasome (100 nM) in the presence of TXNL1 (5 μM) and the absence or presence of arsenite (1 mM). b) The ubiquitin-cleavage activity of the isolated Rpn11/Rpn8 heterodimer is inhibited by TXNL1 or a peptide TNMNDFKRVVGKKGESH representing the last 17 residues of TXNL1’s C-terminus. Shown are the relative activities in ubiquitin-Lys-TAMRA cleavage by Rpn11/Rpn8 in the presence of 633 μM TXNL1 or C-terminal peptide compared to Rpn11/Rpn8 alone (shown are the mean +/− SD for n = 3 technical replicates).
