Supplementary Materials
This PDF file includes:
- Fig. S1. Characterization of UBE2S colocalization and self-association.
- Fig. S2. Characterization of UBE2S cross-linking in cells and in vitro.
- Fig. S3. bBBr-based cross-linking kinetics of UBE2S dimer interface variants.
- Fig. S4. bBBr-based cross-linking kinetics of additional UBE2S variants.
- Fig. S5. Effect of the C-helix on the UBC domain of UBE2S.
- Fig. S6. Mass spectrometric analyses of bBBr-based UBE2S cross-linking.
- Fig. S7. NMR-based comparison of the interactions between UBE2S variants and ubiquitin.
- Fig. S8. Activity assays with UBE2S wild-type and dimer interface variants.
- Fig. S9. Characterization of UBE2S dimer interface variants in cells and in vitro.
- Table S1. Peak list for the deconvoluted mass spectrum shown in fig. S6A.
- Table S2. Mapping of bBBr-cross-linking sites in the UBE2S dimer by ESI-MS shown in fig. S6C.
- Table S3. Plasmids, primers, and cloning information.
- Table S4. Antibodies.
- References (72, 73)
