DSS1/Sem1, a multifunctional and intrinsically disordered protein

Birthe Brandt Kragelund, Signe Marie Schenstrøm, Caio A. Rebula, Vikram Govind Panse, Rasmus Hartmann-Petersen

19 Citationer (Scopus)

Abstract

DSS1/Sem1 is a versatile intrinsically disordered protein. Besides being a bona fide subunit of the 26S proteasome, DSS1 associates with other protein complexes, including BRCA2-RPA, involved in homologous recombination; the Csn12-Thp3 complex, involved in RNA splicing; the integrator, involved in transcription; and the TREX-2 complex, involved in nuclear export of mRNA and transcription elongation. As a subunit of the proteasome, DSS1 functions both in complex assembly and possibly as a ubiquitin receptor. Here, we summarise structural and functional aspects of DSS1/Sem1 with particular emphasis on its multifunctional and disordered properties. We suggest that DSS1/Sem1 can act as a polyanionic adhesive to prevent nonproductive interactions during construction of protein assemblies, uniquely employing different structures when associating with the diverse multisubunit complexes.

OriginalsprogEngelsk
TidsskriftTrends in Biochemical Sciences
Vol/bind41
Udgave nummer5
Sider (fra-til)446-459
Antal sider14
ISSN0968-0004
DOI
StatusUdgivet - 1 maj 2016

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