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Expanded Interactome of the Intrinsically Disordered Protein Dss1.

ABSTRACT: 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.

SUBMITTER: Schenstrom SM

PROVIDER: S-EPMC6218214 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Expanded Interactome of the Intrinsically Disordered Protein Dss1.

Schenstrøm Signe M SM Rebula Caio A CA Tatham Michael H MH Hendus-Altenburger Ruth R Jourdain Isabelle I Hay Ronald T RT Kragelund Birthe B BB Hartmann-Petersen Rasmus R

Cell reports 20181001 4

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, Ds ...[more]

PMID: 30355493

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