Purification and identification of endogenous polySUMO conjugates

Roland Bruderer, Michael H. Tatham, Anna Plechanovova, Ivan Matic, Amit K. Garg, Ronald T. Hay

    Research output: Contribution to journalArticlepeer-review

    135 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)142-148
    Number of pages7
    JournalEMBO Reports
    Issue number2
    Publication statusPublished - Feb 2011


    • SUMO
    • polySUMO
    • SUMO substrates
    • affinity purification
    • mass spectrometry
    • CHAINS
    • PCNA
    • DNA


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