ArticleJournal of bacteriology2000
Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed, 79 citations in OpenAlex.
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Proteolytic Activity of DegP Is Required for theMicrobiology spectrum · 2023Article
- Structural basis of DegP protease temperature-dependent activation.Science advances · 2021Article
- Stress-Responsive Periplasmic Chaperones in Bacteria.Frontiers in molecular biosciences · 2021Review
- Complex Response of the CpxAR Two-Component System to β-Lactams on Antibiotic Resistance and Envelope Homeostasis inAntimicrobial agents and chemotherapy · 2020Article
- Suppressor Mutations inJournal of bacteriology · 2019Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition.The Journal of biological chemistry · 2018Article
- Article
- Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditions.Journal of bacteriology · 2014Article
- Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The Bam machine: a molecular cooper.Biochimica et biophysica acta · 2012Review
- The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportation.Journal of bacteriology · 2012Article
- Article
- Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.EcoSal Plus · 2011Article
- Article
- Involvement of the Shewanella oneidensis decaheme cytochrome MtrA in the periplasmic stability of the beta-barrel protein MtrB.Applied and environmental microbiology · 2011Article
- Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis.PloS one · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Replacement of OmpF's conserved carboxy-terminal phenylalanine with dissimilar amino acids severely impaired its assembly into stable trimers. In some instances, interactions of mutant proteins with the outer membrane were also affected, as judged by their hypersensitivity phenotype. Synthesis of all mutant OmpF proteins elevated the expression of periplasmic protease DegP, and synthesis of most of them made its presence obligatory for cell viability. These results showed a critical role for DegP in the event of aberrant outer membrane protein assembly. The lethal phenotype of mutant OmpF proteins in a degP null background was eliminated when a protease-deficient DegP(S210A) protein was overproduced. Our data showed that this rescue from lethality and a subsequent increase in mutant protein levels in the envelope did not lead to the proper assembly of the mutant proteins in the outer membrane. Rather, a detergent-soluble and thermolabile OmpF species resembling monomers accumulated in the mutants, and to a lesser extent in the parental strain, when DegP(S210A) was overproduced. Interestingly, this also led to the localization of a significant amount of mutant polypeptides to the inner membrane, where DegP(S210A) also fractionated. These results suggested that the DegP(S210A)-mediated rescue from toxicity involved preferential sequestration of misfolded OmpF monomers from the normal assembly pathway.
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What OpenQuestion holds
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.