DSS1/Sem1, a multifunctional and intrinsically disordered protein
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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.
Originalsprog | Engelsk |
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Tidsskrift | Trends in Biochemical Sciences |
Vol/bind | 41 |
Udgave nummer | 5 |
Sider (fra-til) | 446-459 |
Antal sider | 14 |
ISSN | 0968-0004 |
DOI | |
Status | Udgivet - 2016 |
ID: 161363029