dc.identifier.uri |
http://dx.doi.org/10.15488/4715 |
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dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/4757 |
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dc.contributor.author |
Brüser, Thomas
|
ger |
dc.contributor.author |
Heidrich, Eyleen Sabine
|
ger |
dc.date.accessioned |
2019-04-17T09:21:44Z |
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dc.date.available |
2019-04-17T09:21:44Z |
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dc.date.issued |
2018 |
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dc.identifier.citation |
Heidrich, E.S.; Brüser, T.: Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA. In: PLoS ONE 13 (2018), Nr. 6, e0198564. DOI: https://doi.org/10.1371/journal.pone.0198564 |
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dc.description.abstract |
PspA is a key component of the bacterial Psp membrane-stress response system. The biochemical and functional characterization of PspA is impeded by its oligomerization and aggregation properties. It was recently possible to solve the coiled coil structure of a completely soluble PspA fragment, PspA(1–144), that associates with the σ54 enhancer binding protein PspF at its W56-loop and thereby down-regulates the Psp response. We now found that the C-terminal part of PspA, PspA(145–222), also interacts with PspF and inhibits its activity in the absence of full-length PspA. Surprisingly, PspA(145–222) effects changed completely in the presence of full-length PspA, as promoter activity was triggered instead of being inhibited under this condition. PspA(145–222) thus interfered with the inhibitory effect of full-length PspA on PspF, most likely by interacting with full-length PspA that remained bound to PspF. In support of this view, a comprehensive bacterial-2-hybrid screen as well as co-purification analyses indicated a self-interaction of PspA(145–222) and an interaction with full-length PspA. This is the first direct demonstration of PspA/PspA and PspA/PspF interactions in vivo that are mediated by the C-terminus of PspA. The data indicate that regulatory binding sites on PspF do not only exist for the N-terminal coiled coil domain but also for the C-terminal domain of PspA. The inhibition of PspF by PspA-(145–222) was reduced upon membrane stress, whereas the inhibition of PspF by PspA(1–144) did not respond to membrane stress. We therefore propose that the C-terminal domain of PspA is crucial for the regulation of PspF in response to Psp system stimuli. |
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dc.language.iso |
eng |
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dc.publisher |
San Francisco : Public Library of Science |
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dc.relation.ispartofseries |
PLoS ONE 13 (2018), Nr. 6 |
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dc.rights |
CC BY 4.0 Unported |
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dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
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dc.subject |
Protein domains |
eng |
dc.subject |
Microbiology |
eng |
dc.subject |
Protein structure |
eng |
dc.subject |
bacterial Psp |
eng |
dc.subject.ddc |
570 | Biowissenschaften, Biologie
|
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dc.title |
Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA |
eng |
dc.type |
Article |
ger |
dc.type |
Text |
ger |
dc.relation.essn |
1932-6203 |
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dc.relation.doi |
10.1371/journal.pone.0198564 |
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dc.bibliographicCitation.firstPage |
e0198564 |
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dc.description.version |
publishedVersion |
ger |
tib.accessRights |
frei zug�nglich |
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