Literature DB >> 26944332

DSS1/Sem1, a Multifunctional and Intrinsically Disordered Protein.

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.
Copyright © 2016 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  DNA repair; PCI domain; intrinsically disordered proteins; mRNA export; proteasome; protein degradation

Mesh:

Substances:

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


  22 in total

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