ArticleJournal of bacteriology2011
FtsH-dependent degradation of phage shock protein C in Yersinia enterocolitica and Escherichia coli.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 15 citations in OpenAlex.
- Essential Role of LapD in the Absence of Cardiolipins.International journal of molecular sciences · 2026Article
- An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins.The EMBO journal · 2025Article
- An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins.bioRxiv : the preprint server for biology · 2024Article
- Bacterial rhomboid proteases mediate quality control of orphan membrane proteins.The EMBO journal · 2020Article
- Article
- Conditional Proteolysis of the Membrane Protein YfgM by the FtsH Protease Depends on a Novel N-terminal Degron.The Journal of biological chemistry · 2015Article
- Activity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners.The Journal of biological chemistry · 2015Article
- Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein response.Molecular microbiology · 2013Article
- A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.The Journal of biological chemistry · 2012Article
- Phage shock protein C (PspC) of Yersinia enterocolitica is a polytopic membrane protein with implications for regulation of the Psp stress response.Journal of bacteriology · 2012Article
- Phage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica.Molecular microbiology · 2012Article
- Recent findings about the Yersinia enterocolitica phage shock protein response.Journal of microbiology (Seoul, Korea) · 2012Review
- Links between type III secretion and extracytoplasmic stress responses in Yersinia.Frontiers in cellular and infection microbiology · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The widely conserved phage shock protein (Psp) extracytoplasmic stress response has been studied extensively in Escherichia coli and Yersinia enterocolitica. Both species have the PspF, -A, -B, and -C proteins, which have been linked to robust phenotypes, including Y. enterocolitica virulence. PspB and PspC are cytoplasmic membrane proteins required for stress-dependent induction of psp gene expression and for bacterial survival during the mislocalization of outer membrane secretin proteins. Previously, we reported that Y. enterocolitica PspB functions to positively control the amount of PspC by an uncharacterized posttranscriptional mechanism. In this study, we have discovered that the cytoplasmic membrane protease FtsH is involved in this phenomenon. FtsH destabilizes PspC in Y. enterocolitica, but coproduction of PspC with its binding partner PspB was sufficient to prevent this destabilization. In contrast, FtsH did not affect any other core component of the Psp system. These data suggested that uncomplexed PspC might be particularly deleterious to the bacterial cell and that FtsH acts as an important quality control mechanism to remove it. This was supported by the observation that toxicity caused by PspC production was reduced either by coproduction of PspB or by increased synthesis of FtsH. We also found that the phenomenon of FtsH-dependent PspC destabilization is conserved between Y. enterocolitica and E. coli.
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Registered trials
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.