Regulation of the 26S Proteasome Complex During Oxidative Stress

Xiaorong Wang, James Yen, Peter Kaiser,* Lan Huang*

*To whom correspondence should be addressed. E-mail: lanhuang{at}uci.edu (L.H.); pkaiser{at}uci.edu (P.K.)

This PDF file includes:

• Fig. S1. Average SILAC ratios (L/H) of the yeast 19S and 20S subunits purified with the 20S subunit Pre10-TAP after oxidative stress.
• Fig. S2. Quantitative comparison of the composition of the 26S proteasome purified by Rpn11-TAP from wild-type and ecm29Δ cells with the SILAC-MS method.
• Fig. S3. Yap1-independent enrichment of Ecm29 in purified 19S complexes.
• Fig. S4. In-gel proteasome activities in ecm29Δ cells after H₂O₂-induced stress.
• Fig. S5. Validation of H₂O₂-triggered separation of the 20S core from the 19S particle in human cells by Western blotting analysis.
• Fig. S6. Presence of Ecm29 in purified 19S subunits is independent of the salt concentration used during affinity purification.
• Fig. S7. Reassembly of the 26S proteasome after 3 mM H₂O₂-induced stress.
• Table S1. Identification and quantitation of proteasome subunits by SILAC-MS in Rpn11-TAP–expressing cells before and after treatment with H₂O₂.
• Table S2. Identification and quantitation of proteasome subunits and Ecm29 by SILAC-MS in Pre10-TAP–expressing cells before and after treatment with H₂O₂.
• Table S3. Identification and quantitation of the known PIPs by SILAC-MS in Rpn11-TAP–expressing cells before and after treatment with H₂O₂.
• Table S4. SILAC-based quantitative comparison of the composition of the 26S proteasome in wild-type and ecm29Δ cells in the absence of H₂O₂-induced stress.
• Table S5. SILAC-based quantitative comparison of the composition of the 26S proteasome in wild-type and ecm29Δ cells after H₂O₂-induced stress.
• Table S6. Yeast strains generated for this study.
  

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