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)

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