Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4

Yingqi Xu, Anna Plechanovová, Peter Simpson, Jan Marchant, Orsolya Leidecker, Sebastian Kraatz, Ronald T. Hay (Lead / Corresponding author), Steve J. Matthews (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    16 Citations (Scopus)
    201 Downloads (Pure)


    The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer.
    Original languageEnglish
    Article number4217
    Number of pages12
    JournalNature Communications
    Publication statusPublished - 27 Jun 2014


    Cite this