ArticleProteomics2012
Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics.
Article in Proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
47 citing papers in PubMed, 67 citations in OpenAlex.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- Liganded LolCDE structures reveal a common substrate-LolE interaction guiding bacterial lipoprotein transport.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.Nature communications · 2026Article
- Identification of host genetic factors modulating β-lactam resistance inEmerging microbes & infections · 2025Article
- Architecture and conformational dynamics of the BAM-SurA holo insertase complex.Science advances · 2025Article
- A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.Cell host & microbe · 2025Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target.Molecules (Basel, Switzerland) · 2023Review
- Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The sacrificial adaptor protein Skp functions to remove stalled substrates from the β-barrel assembly machine.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The periplasmic chaperone Skp prevents misfolding of the secretory lipase A fromFrontiers in molecular biosciences · 2022Article
- Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms.mBio · 2021Article
- Defects in The First Step of Lipoprotein Maturation Underlie The Synthetic Lethality ofJournal of bacteriology · 2021Article
- SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA.Protein science : a publication of the Protein Society · 2020Article
- The transmembrane supercomplex mediating the biogenesis of OMPs in Gram-negative bacteria assumes a circular conformational change upon activation.FEBS open bio · 2020Article
- Loss of the Periplasmic Chaperone Skp and Mutations in the Efflux Pump AcrAB-TolC Play a Role in Acquired Resistance to Antimicrobial Peptides inFrontiers in microbiology · 2020Article
- Genome-scale model of metabolism and gene expression provides a multi-scale description of acid stress responses in Escherichia coli.PLoS computational biology · 2019Article
- Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.Molecular microbiology · 2019Article
- The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT.Journal of molecular biology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
β-Barrel proteins, or outer membrane proteins (OMPs), perform many essential functions in Gram-negative bacteria, but questions remain about the mechanism by which they are assembled into the outer membrane (OM). In Escherichia coli, β-barrels are escorted across the periplasm by chaperones, most notably SurA and Skp. However, the contributions of these two chaperones to the assembly of the OM proteome remained unclear. We used differential proteomics to determine how the elimination of Skp and SurA affects the assembly of many OMPs. We have shown that removal of Skp has no impact on the levels of the 63 identified OM proteins. However, depletion of SurA in the skp strain has a marked impact on the OM proteome, diminishing the levels of almost all β-barrel proteins. Our results are consistent with a model in which SurA plays a primary chaperone role in E. coli. Furthermore, they suggest that while no OMPs prefer the Skp chaperone pathway in wild-type cells, most can use Skp efficiently when SurA is absent. Our data, which provide a unique glimpse into the protein content of the nonviable surA skp mutant, clarify the roles of the periplasmic chaperones in E. coli.
Indexed as
Identifiers
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.