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

Download statistics - Document (COUNTER):

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

Repository version

To cite the version in the repository, please use this identifier: https://doi.org/10.15488/4715

Selected time period:

year: 
month: 

Sum total of downloads: 37




Thumbnail
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.
License of this version: CC BY 4.0 Unported
Document Type: article
Publishing status: publishedVersion
Issue Date: 2018
Appears in Collections:Naturwissenschaftliche Fakultät

distribution of downloads over the selected time period:

downloads by country:

pos. country downloads
total perc.
1 image of flag of Germany Germany 35 94.59%
2 image of flag of United States United States 2 5.41%

Further download figures and rankings:


Hinweis

Zur Erhebung der Downloadstatistiken kommen entsprechend dem „COUNTER Code of Practice for e-Resources“ international anerkannte Regeln und Normen zur Anwendung. COUNTER ist eine internationale Non-Profit-Organisation, in der Bibliotheksverbände, Datenbankanbieter und Verlage gemeinsam an Standards zur Erhebung, Speicherung und Verarbeitung von Nutzungsdaten elektronischer Ressourcen arbeiten, welche so Objektivität und Vergleichbarkeit gewährleisten sollen. Es werden hierbei ausschließlich Zugriffe auf die entsprechenden Volltexte ausgewertet, keine Aufrufe der Website an sich.

Search the repository


Browse