A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA+ Transcription Activator Protein PspF for Negative Regulation
dc.contributor.author | Joly, N | |
dc.contributor.author | Burrows, PC | |
dc.contributor.author | Engl, C | |
dc.contributor.author | Jovanovic, G | |
dc.contributor.author | Buck, M | |
dc.date.accessioned | 2020-06-03T08:48:28Z | |
dc.date.available | 2020-06-03T08:48:28Z | |
dc.date.issued | 2009-12 | |
dc.identifier.citation | Joly, N., Burrows, P., Engl, C., Jovanovic, G. and Buck, M., 2009. A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA+ Transcription Activator Protein PspF for Negative Regulation. Journal of Molecular Biology, [online] 394(4), pp.764-775. Available at: <https://www.sciencedirect.com/science/article/pii/S0022283609011942?via%3Dihub> [Accessed 3 June 2020]. | en_US |
dc.identifier.issn | 0022-2836 | |
dc.identifier.uri | https://qmro.qmul.ac.uk/xmlui/handle/123456789/64606 | |
dc.description.abstract | To survive and colonise their various environments, including those used during infection, bacteria have developed a variety of adaptive systems. Amongst these is phage shock protein (Psp) response, which can be induced in Escherichia coli upon filamentous phage infection (specifically phage secretin pIV) and by other membrane-damaging agents. The E. coli Psp system comprises seven proteins, of which PspA is the central component. PspA is a bifunctional protein that is directly involved in (i) the negative regulation of the psp-specific transcriptional activator PspF and (ii) the maintenance of membrane integrity in a mechanism proposed to involve the formation of a 36-mer ring complex. Here we established that the PspA negative regulation of PspF ATPase activity is the result of a cooperative inhibition. We present biochemical evidence showing that an inhibitory PspA–PspF regulatory complex, which has significantly reduced PspF ATPase activity, is composed of around six PspF subunits and six PspA subunits, suggesting that PspA exists in at least two different oligomeric assemblies. We now establish that all four putative helical domains of PspA are critical for the formation of the 36-mer. In contrast, not all four helical domains are required for the formation of the inhibitory PspA–PspF complex. Since a range of initial PspF oligomeric states permit formation of the apparent PspA–PspF dodecameric assembly, we conclude that PspA and PspF demonstrate a strong propensity to self-assemble into a single defined heteromeric regulatory complex. | en_US |
dc.format.extent | 764 - 775 | |
dc.language | en | |
dc.publisher | Elsevier BV | en_US |
dc.relation.ispartof | Journal of Molecular Biology | |
dc.rights | This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. | |
dc.rights | Attribution 3.0 United States | * |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/us/ | * |
dc.title | A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA+ Transcription Activator Protein PspF for Negative Regulation | en_US |
dc.type | Article | en_US |
dc.rights.holder | © 2009 Elsevier Ltd. | |
dc.identifier.doi | 10.1016/j.jmb.2009.09.055 | |
pubs.issue | 4 | en_US |
pubs.notes | Not known | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 394 | en_US |
rioxxterms.funder | Default funder | en_US |
rioxxterms.identifier.project | Default project | en_US |
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