Expanded Interactome of the Intrinsically Disordered Protein Dss1

Signe M. Schenstrøm, Caio A. Rebula, Michael H. Tatham, Ruth Hendus-Altenburger, Isabelle Jourdain, Ronald T. Hay, Birthe B. Kragelund, Rasmus Hartmann-Petersen (Lead / Corresponding author)

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8 Citations (Scopus)
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Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes. Accordingly, Dss1 functions in protein degradation, DNA repair, transcription, and mRNA export. Here in Schizosaccharomyces pombe, we expand its interactome further to include eIF3, the COP9 signalosome, and the mitotic septins. Within its intrinsically disordered ensemble, Dss1 forms a transiently populated C-terminal helix that dynamically interacts with and shields a central binding region. The helix interfered with the interaction to ATP-citrate lyase but was required for septin binding, and in strains lacking Dss1, ATP-citrate lyase solubility was reduced and septin rings were more persistent. Thus, even weak, transient interactions within Dss1 may dynamically rewire its interactome.

Original languageEnglish
Pages (from-to)862-870
Number of pages9
JournalCell Reports
Issue number4
Early online date23 Oct 2018
Publication statusPublished - 23 Oct 2018


  • PCI domain
  • intrinsically disordered proteins
  • proteasome
  • protein degradation


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