The dynamics of linear polyubiquitin

Research output: Contribution to journal › Journal article › Research › peer-review

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The dynamics of linear polyubiquitin. / Jussupow, Alexander; Messias, Ana C.; Stehle, Ralf; Geerlof, Arie; Solbak, Sara Marie Øie; Paissoni, Cristina; Bach, Anders; Sattler, Michael; Camilloni, Carlo.

In: Science Advances, Vol. 6, No. 42, eabc3786, 10.2020.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Jussupow, A, Messias, AC, Stehle, R, Geerlof, A, Solbak, SMØ, Paissoni, C, Bach, A, Sattler, M & Camilloni, C 2020, 'The dynamics of linear polyubiquitin', Science Advances, vol. 6, no. 42, eabc3786. https://doi.org/10.1126/sciadv.abc3786

APA

Jussupow, A., Messias, A. C., Stehle, R., Geerlof, A., Solbak, S. M. Ø., Paissoni, C., Bach, A., Sattler, M., & Camilloni, C. (2020). The dynamics of linear polyubiquitin. Science Advances, 6(42), [eabc3786]. https://doi.org/10.1126/sciadv.abc3786

Vancouver

Jussupow A, Messias AC, Stehle R, Geerlof A, Solbak SMØ, Paissoni C et al. The dynamics of linear polyubiquitin. Science Advances. 2020 Oct;6(42). eabc3786. https://doi.org/10.1126/sciadv.abc3786

Author

Jussupow, Alexander ; Messias, Ana C. ; Stehle, Ralf ; Geerlof, Arie ; Solbak, Sara Marie Øie ; Paissoni, Cristina ; Bach, Anders ; Sattler, Michael ; Camilloni, Carlo. / The dynamics of linear polyubiquitin. In: Science Advances. 2020 ; Vol. 6, No. 42.

Bibtex

@article{42efedf214ad4d1292b0c00ab720b423,
title = "The dynamics of linear polyubiquitin",
abstract = "Polyubiquitin chains are flexible multidomain proteins, whose conformational dynamics enable them to regulate multiple biological pathways. Their dynamic is determined by the linkage between ubiquitins and by the number of ubiquitin units. Characterizing polyubiquitin behavior as a function of their length is hampered because of increasing system size and conformational variability. Here, we introduce a new approach to efficiently integrating small-angle x-ray scattering with simulations allowing us to accurately characterize the dynamics of linear di-, tri-, and tetraubiquitin in the free state as well as of diubiquitin in complex with NEMO, a central regulator in the NF-B pathway. Our results show that the behavior of the diubiquitin subunits is independent of the presence of additional ubiquitin modules and that the dynamics of polyubiquitins with different lengths follow a simple model. Together with experimental data from multiple biophysical techniques, we then rationalize the 2:1 NEMO:polyubiquitin binding.",
author = "Alexander Jussupow and Messias, {Ana C.} and Ralf Stehle and Arie Geerlof and Solbak, {Sara Marie {\O}ie} and Cristina Paissoni and Anders Bach and Michael Sattler and Carlo Camilloni",
year = "2020",
month = oct,
doi = "10.1126/sciadv.abc3786",
language = "English",
volume = "6",
journal = "Science advances",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "42",

}

RIS

TY - JOUR

T1 - The dynamics of linear polyubiquitin

AU - Jussupow, Alexander

AU - Messias, Ana C.

AU - Stehle, Ralf

AU - Geerlof, Arie

AU - Solbak, Sara Marie Øie

AU - Paissoni, Cristina

AU - Bach, Anders

AU - Sattler, Michael

AU - Camilloni, Carlo

PY - 2020/10

Y1 - 2020/10

N2 - Polyubiquitin chains are flexible multidomain proteins, whose conformational dynamics enable them to regulate multiple biological pathways. Their dynamic is determined by the linkage between ubiquitins and by the number of ubiquitin units. Characterizing polyubiquitin behavior as a function of their length is hampered because of increasing system size and conformational variability. Here, we introduce a new approach to efficiently integrating small-angle x-ray scattering with simulations allowing us to accurately characterize the dynamics of linear di-, tri-, and tetraubiquitin in the free state as well as of diubiquitin in complex with NEMO, a central regulator in the NF-B pathway. Our results show that the behavior of the diubiquitin subunits is independent of the presence of additional ubiquitin modules and that the dynamics of polyubiquitins with different lengths follow a simple model. Together with experimental data from multiple biophysical techniques, we then rationalize the 2:1 NEMO:polyubiquitin binding.

AB - Polyubiquitin chains are flexible multidomain proteins, whose conformational dynamics enable them to regulate multiple biological pathways. Their dynamic is determined by the linkage between ubiquitins and by the number of ubiquitin units. Characterizing polyubiquitin behavior as a function of their length is hampered because of increasing system size and conformational variability. Here, we introduce a new approach to efficiently integrating small-angle x-ray scattering with simulations allowing us to accurately characterize the dynamics of linear di-, tri-, and tetraubiquitin in the free state as well as of diubiquitin in complex with NEMO, a central regulator in the NF-B pathway. Our results show that the behavior of the diubiquitin subunits is independent of the presence of additional ubiquitin modules and that the dynamics of polyubiquitins with different lengths follow a simple model. Together with experimental data from multiple biophysical techniques, we then rationalize the 2:1 NEMO:polyubiquitin binding.

U2 - 10.1126/sciadv.abc3786

DO - 10.1126/sciadv.abc3786

M3 - Journal article

C2 - 33055165

AN - SCOPUS:85093481472

VL - 6

JO - Science advances

JF - Science advances

SN - 2375-2548

IS - 42

M1 - eabc3786

ER -

ID: 251360449