ArticleJournal of bacteriology2005
Molecular determinants for PspA-mediated repression of the AAA transcriptional activator PspF.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 59 citations in OpenAlex.
- Engineered Phage Enables Efficient Control of Gene Expression upon Infection of the Host Cell.International journal of molecular sciences · 2024Article
- The phage shock protein (PSP) envelope stress response: discovery of novel partners and evolutionary history.mSystems · 2024Article
- Reversible conjugation of a CBASS nucleotide cyclase regulates bacterial immune response to phage infection.Nature microbiology · 2024Article
- Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.Cell · 2021Article
- The route to transcription initiation determines the mode of transcriptional bursting in E. coli.Nature communications · 2020Article
- Envelope stress responses: balancing damage repair and toxicity.Nature reviews. Microbiology · 2019Review
- The Fusion Activity of IM30 Rings Involves Controlled Unmasking of the Fusogenic Core.Frontiers in plant science · 2019Article
- Association of Mycobacterium Proteins with Lipid Droplets.Journal of bacteriology · 2018Article
- Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA.PloS one · 2018Article
- Evaluating the role of phage-shock protein A in Burkholderia pseudomallei.Microbiology (Reading, England) · 2015Article
- Article
- Molecular basis of nucleotide-dependent substrate engagement and remodeling by an AAA+ activator.Nucleic acids research · 2014Article
- A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation.Journal of molecular biology · 2013Article
- The first α-helical domain of the vesicle-inducing protein in plastids 1 promotes oligomerization and lipid binding.Planta · 2013Article
- The role of bacterial enhancer binding proteins as specialized activators of σ54-dependent transcription.Microbiology and molecular biology reviews : MMBR · 2012Review
- The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.The Journal of biological chemistry · 2012Article
- The evolution of the phage shock protein response system: interplay between protein function, genomic organization, and system function.Molecular biology and evolution · 2011Article
- Measuring the stoichiometry of functional PspA complexes in living bacterial cells by single molecule photobleaching.Chemical communications (Cambridge, England) · 2011Article
- Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli.Microbiology (Reading, England) · 2010Article
- A prehydrolysis state of an AAA+ ATPase supports transcription activation of an enhancer-dependent RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Escherichia coli phage shock protein system (pspABCDE operon and pspG gene) is induced by numerous stresses related to the membrane integrity state. Transcription of the psp genes requires the RNA polymerase containing the sigma(54) subunit and the AAA transcriptional activator PspF. PspF belongs to an atypical class of sigma(54) AAA activators in that it lacks an N-terminal regulatory domain and is instead negatively regulated by another regulatory protein, PspA. PspA therefore represses its own expression. The PspA protein is distributed between the cytoplasm and the inner membrane fraction. In addition to its transcriptional inhibitory role, PspA assists maintenance of the proton motive force and protein export. Several lines of in vitro evidence indicate that PspA-PspF interactions inhibit the ATPase activity of PspF, resulting in the inhibition of PspF-dependent gene expression. In this study, we characterize sequences within PspA and PspF crucial for the negative effect of PspA upon PspF. Using a protein fragmentation approach, we show that the integrity of the three putative N-terminal alpha-helical domains of PspA is crucial for the role of PspA as a negative regulator of PspF. A bacterial two-hybrid system allowed us to provide clear evidence for an interaction in E. coli between PspA and PspF in vivo, which strongly suggests that PspA-directed inhibition of PspF occurs via an inhibitory complex. Finally, we identify a single PspF residue that is a binding determinant for PspA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.