Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA

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dc.identifier.uri http://dx.doi.org/10.15488/4715
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/4757
dc.contributor.author Brüser, Thomas ger
dc.contributor.author Heidrich, Eyleen Sabine ger
dc.date.accessioned 2019-04-17T09:21:44Z
dc.date.available 2019-04-17T09:21:44Z
dc.date.issued 2018
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 ger
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. ger
dc.language.iso eng ger
dc.publisher San Francisco : Public Library of Science
dc.relation.ispartofseries PLoS ONE 13 (2018), Nr. 6 ger
dc.rights CC BY 4.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
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 ger
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
dc.relation.doi 10.1371/journal.pone.0198564
dc.description.version publishedVersion ger
tib.accessRights frei zug�nglich

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