Expanded Interactome of the Intrinsically Disordered Protein Dss1

TY - JOUR

T1 - Expanded Interactome of the Intrinsically Disordered Protein Dss1

AU - Schenstrøm, Signe M.

AU - Rebula, Caio A.

AU - Tatham, Michael H.

AU - Hendus-Altenburger, Ruth

AU - Jourdain, Isabelle

AU - Hay, Ronald T.

AU - Kragelund, Birthe B.

AU - Hartmann-Petersen, Rasmus

N1 - Copyright © 2018 The Author(s). Published by Elsevier Inc. All rights reserved.

PY - 2018/10/23

Y1 - 2018/10/23

N2 - 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.

AB - 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.

KW - PCI domain

KW - intrinsically disordered proteins

KW - proteasome

KW - protein degradation

UR - https://www.scopus.com/pages/publications/85054766333

U2 - 10.1016/j.celrep.2018.09.080

DO - 10.1016/j.celrep.2018.09.080

M3 - Article

C2 - 30355493

SN - 2211-1247

VL - 25

SP - 862

EP - 870

JO - Cell Reports

JF - Cell Reports

IS - 4

ER -