dc.identifier.uri |
http://dx.doi.org/10.15488/10950 |
|
dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/11032 |
|
dc.contributor.author |
Mahieu, Emilie
|
|
dc.contributor.author |
Covès, Jaques
|
|
dc.contributor.author |
Krüger, Georg
|
|
dc.contributor.author |
Martel, Anne
|
|
dc.contributor.author |
Moulin, Martine
|
|
dc.contributor.author |
Carl, Nico
|
|
dc.contributor.author |
Härtlein, Michael
|
|
dc.contributor.author |
Carlomagno, Teresa
|
|
dc.contributor.author |
Franzetti, Bruno
|
|
dc.contributor.author |
Gabel, Frank
|
|
dc.date.accessioned |
2021-05-18T09:29:23Z |
|
dc.date.available |
2021-05-18T09:29:23Z |
|
dc.date.issued |
2020 |
|
dc.identifier.citation |
Mahieu, E.; Covès, J.; Krüger, G.; Martel, A.; Moulin, M. et al.: Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering. In: Biophysical Journal 119 (2020), Nr. 2, S. 375-388. DOI: https://doi.org/10.1016/j.bpj.2020.06.015 |
|
dc.description.abstract |
The proteasome is a key player of regulated protein degradation in all kingdoms of life. Although recent atomic structures have provided snapshots on a number of conformations, data on substrate states and populations during the active degradation process in solution remain scarce. Here, we use time-resolved small-angle neutron scattering of a deuterium-labeled GFPssrA substrate and an unlabeled archaeal PAN-20S system to obtain direct structural information on substrate states during ATP-driven unfolding and subsequent proteolysis in solution. We find that native GFPssrA structures are degraded in a biexponential process, which correlates strongly with ATP hydrolysis, the loss of fluorescence, and the buildup of small oligopeptide products. Our solution structural data support a model in which the substrate is directly translocated from PAN into the 20S proteolytic chamber, after a first, to our knowledge, successful unfolding process that represents a point of no return and thus prevents dissociation of the complex and the release of harmful, aggregation-prone products. © 2020 Biophysical Society |
eng |
dc.language.iso |
eng |
|
dc.publisher |
Cambridge, MA : Cell Press |
|
dc.relation.ispartofseries |
Biophysical Journal 119 (2020), Nr. 2 |
|
dc.rights |
CC BY-NC-ND 4.0 Unported |
|
dc.rights.uri |
https://creativecommons.org/licenses/by-nc-nd/4.0/ |
|
dc.subject |
hydrolysis |
eng |
dc.subject |
fluorescence |
eng |
dc.subject |
ATP |
eng |
dc.subject |
protein |
eng |
dc.subject |
PAN-20S |
eng |
dc.subject.ddc |
570 | Biowissenschaften, Biologie
|
ger |
dc.title |
Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering |
|
dc.type |
Article |
|
dc.type |
Text |
|
dc.relation.essn |
1542-0086 |
|
dc.relation.issn |
0006-3495 |
|
dc.relation.doi |
https://doi.org/10.1016/j.bpj.2020.06.015 |
|
dc.bibliographicCitation.issue |
2 |
|
dc.bibliographicCitation.volume |
119 |
|
dc.bibliographicCitation.firstPage |
375 |
|
dc.bibliographicCitation.lastPage |
388 |
|
dc.description.version |
publishedVersion |
|
tib.accessRights |
frei zug�nglich |
|