TY - JOUR
T1 - DSS1/Sem1, a multifunctional and intrinsically disordered protein
AU - Kragelund, Birthe Brandt
AU - Schenstrøm, Signe Marie
AU - Rebula, Caio A.
AU - Panse, Vikram Govind
AU - Hartmann-Petersen, Rasmus
N1 - Copyright © 2016 Elsevier Ltd. All rights reserved.
PY - 2016/5/1
Y1 - 2016/5/1
N2 - 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.
AB - 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.
U2 - 10.1016/j.tibs.2016.02.004
DO - 10.1016/j.tibs.2016.02.004
M3 - Journal article
C2 - 26944332
SN - 0968-0004
VL - 41
SP - 446
EP - 459
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 5
ER -