DSS1/Sem1, a multifunctional and intrinsically disordered protein

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DSS1/Sem1, a multifunctional and intrinsically disordered protein. / Kragelund, Birthe Brandt; Schenstrøm, Signe Marie; Rebula, Caio A.; Panse, Vikram Govind; Hartmann-Petersen, Rasmus.

I: Trends in Biochemical Sciences, Bind 41, Nr. 5, 2016, s. 446-459.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Kragelund, BB, Schenstrøm, SM, Rebula, CA, Panse, VG & Hartmann-Petersen, R 2016, 'DSS1/Sem1, a multifunctional and intrinsically disordered protein', Trends in Biochemical Sciences, bind 41, nr. 5, s. 446-459. https://doi.org/10.1016/j.tibs.2016.02.004

APA

Kragelund, B. B., Schenstrøm, S. M., Rebula, C. A., Panse, V. G., & Hartmann-Petersen, R. (2016). DSS1/Sem1, a multifunctional and intrinsically disordered protein. Trends in Biochemical Sciences, 41(5), 446-459. https://doi.org/10.1016/j.tibs.2016.02.004

Vancouver

Kragelund BB, Schenstrøm SM, Rebula CA, Panse VG, Hartmann-Petersen R. DSS1/Sem1, a multifunctional and intrinsically disordered protein. Trends in Biochemical Sciences. 2016;41(5):446-459. https://doi.org/10.1016/j.tibs.2016.02.004

Author

Kragelund, Birthe Brandt ; Schenstrøm, Signe Marie ; Rebula, Caio A. ; Panse, Vikram Govind ; Hartmann-Petersen, Rasmus. / DSS1/Sem1, a multifunctional and intrinsically disordered protein. I: Trends in Biochemical Sciences. 2016 ; Bind 41, Nr. 5. s. 446-459.

Bibtex

@article{b6dd6c8fb4d142c4be0b68ff93f809fb,

title = "DSS1/Sem1, a multifunctional and intrinsically disordered protein",

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.",

author = "Kragelund, {Birthe Brandt} and Schenstr{\o}m, {Signe Marie} and Rebula, {Caio A.} and Panse, {Vikram Govind} and Rasmus Hartmann-Petersen",

year = "2016",

doi = "10.1016/j.tibs.2016.02.004",

language = "English",

volume = "41",

pages = "446--459",

journal = "Trends in Biochemical Sciences",

issn = "0968-0004",

publisher = "Elsevier",

number = "5",

}

RIS

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

PY - 2016

Y1 - 2016

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

VL - 41

SP - 446

EP - 459

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0968-0004

IS - 5

ER -

ID: 161363029