| Literature DB >> 26944332 |
Birthe B Kragelund1, Signe M Schenstrøm1, Caio A Rebula1, Vikram Govind Panse2, Rasmus Hartmann-Petersen3.
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.Entities:
Keywords: DNA repair; PCI domain; intrinsically disordered proteins; mRNA export; proteasome; protein degradation
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Year: 2016 PMID: 26944332 DOI: 10.1016/j.tibs.2016.02.004
Source DB: PubMed Journal: Trends Biochem Sci ISSN: 0968-0004 Impact factor: 13.807