Purification and identification of endogenous polySUMO conjugates

EMBO Rep. 2011 Feb;12(2):142-8. doi: 10.1038/embor.2010.206. Epub 2011 Jan 21.


The small ubiquitin-like modifier (SUMO) can undergo self-modification to form polymeric chains that have been implicated in cellular processes such as meiosis, genome maintenance and stress response. Investigations into the biological role of polymeric chains have been hampered by the absence of a protocol for the purification of proteins linked to SUMO chains. In this paper, we describe a rapid affinity purification procedure for the isolation of endogenous polySUMO-modified species that generates highly purified material suitable for individual protein studies and proteomic analysis. We use this approach to identify more than 300 putative polySUMO conjugates from cultured eukaryotic cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • HeLa Cells
  • Hot Temperature
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism*
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Proteome / isolation & purification*
  • Proteome / metabolism
  • Stress, Physiological
  • Subcellular Fractions / metabolism
  • Sumoylation
  • Transcription Factors / metabolism*


  • Nuclear Proteins
  • Proteome
  • RNF4 protein, human
  • Transcription Factors