Supplementary Materials

The PDF file includes:

  • Fig. S1. Profiling of protein expression and arginine methylation in response to GSK591.
  • Fig. S2. Schematic representation of hmSEEKER workflow.
  • Fig. S3. PRMT5-MEP50 complex is more active than PRMT5.
  • Fig. S4. Validation of PRMT5-MEP50 substrates by in vitro radioactive methylation assay on synthetic peptides.
  • Fig. S5. Substrate specificity of PRMT5 on G24 mutant CNBP proteins.
  • Fig. S6. MS2 spectrum of the hmSILAC-labeled multimethylated peptide of 40S ribosomal proteins S10, carrying two SDMA.
  • Legends for data files S1 to S4
  • Legends for tables S1 to S3

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Other Supplementary Material for this manuscript includes the following:

  • Data file S1 (.pdf format). Neutral loss analysis of hmSILAC dimethyl peptides.
  • Data file S2 (.pdf format). MS2 spectra of all methyl peptides down-regulated by GSK591.
  • Data file S3 (.pdf format). MS2 spectra of all methyl peptides not responding to GSK591.
  • Data file S4 (.pdf format). MS2 spectra of hmSILAC methyl peptides bearing ADMA and SDMA on the same arginine residue.
  • Table S1 (Microsoft Excel format). The dynamic R-methyl proteome in response to GSK591 treatment.
  • Table S2 (Microsoft Excel format). hmSILAC R-methyl peptides used for the orthogonal validation of the SILAC experiment.
  • Table S3 (Microsoft Excel format). Nonredundant lists of SILAC-quantified R-methyl peptides.